Off-target peptide-MHC complex conformation modeling systems and methods for antigen-recognition molecule development

Abstract

A workflow is presented herein which includes methods and computational systems and devices for providing 3D computational models of potential off-target peptides each positioned in a groove of an MHC molecule ("MHC-off-target models"), quantifying structural similarity between each potential off-target peptide to a target peptide based on a comparison of the MHC-off-target models to a 3D computational model of a target MHC-peptide complex ("MHC-target model"), and ranking the potential off-target peptides based on a structural similarity metric. Example methods and systems can be applied to solve bioinformatics and treatment development problems. The present disclosure also relates to compositions that involve isolated peptides, e.g., MAGEA3168-176 and / or WT1126-134 off-target peptides, and the use of such compositions in methods for assessing off-target effects of antigen-recognition molecules that target a MAGEA3168-176 and / or WT1126-134 peptide, as well as for selecting antigen-recognition molecules and enriching samples for antigen-recognition molecules that specifically bind the MAGEA3168-176 and / or WT1126-134.

Description

Attorney Docket #: 250298.000961 OFF-TARGET PEPTIDE-MHC COMPLEX CONFORMATION MODELING SYSTEMS AND METHODS FOR ANTIGEN-RECOGNITION MOLECULE DEVELOPMENT CROSS-REFERENCE TO RELATED APPLICATIONS This application claims priority, and benefit under 35 U.S.C. § 119(e), to U.S. Provisional Application No. 63 / 665,588, filed on June 28, 2024, and entitled “TARGET PEPTIDE-MHC COMPLEX CONFORMATION MODELING SYSTEMS AND METHODS FOR ANTIGEN- RECOGNITION MOLECULE DEVELOPMENT,” the entirety of which is incorporated herein by reference. SEQUENCE LISTING The instant application contains a Sequence Listing which has been submitted electronically in XML format and is hereby incorporated by reference in its entirety. Said XML copy, created on June 20, 2025, is named 250298_000961_SL.xml and is 413,733 bytes in size. FIELD This application relates generally to computational systems and methods for providing 3D computational models of a peptide presented in a complex with a major histocompatibility complex (MHC) molecule (MHC-peptide complex) and comparing such models for the purpose of predicting off-target toxicity associated with potential target MHC-peptide complex(s). BACKGROUND Antigen-recognition molecules, such as T-cell receptors (TCRs) and antibodies, are capable of identifying antigens, which include agents recognized by the immune system of a host as defined herein. Antigen-recognition molecules can help the immune system neutralize an antigen by binding to an antigenic peptide presented in an MHC-peptide complex on the surface of an antigen-presenting cell. The MHC-peptide complex is presented on the surface of the antigen-presenting cell as a result of a cellular process in which an MHC gene in the antigen cell encodes an MHC molecule; the MHC molecule subsequently binds to the antigenic peptide thereby creating the MHC-peptide complex; and the resulting MHC-peptide complex is positioned on the cell surface so that a portionAttorney Docket #: 250298.000961 of the peptide is presented for binding with an antigen-recognition molecule. Each peptide is made up of a short chain of amino acids, and some of the amino acids of a peptide in an MHC-peptide complex are bound to the MHC molecule while at least some of the remaining amino acids are presented as available for binding with an antigen-recognition molecule. This cellular process is also carried out in cells native to the body. Generally, antigen- recognition molecules are able to distinguish between peptides presented on native cells vs. peptides presented on antigen-presenting cells so that normal cells are not attacked by the immune system. Antigen-recognition molecules are able to bind to a peptide of an MHC-peptide complex on the surface of an antigen-presenting cell to help the immune system neutralize the antigen. Research is underway with a goal of engineering antigen-recognition molecules to target cells that would otherwise not be targeted through the above-described mechanism. For instance, cancer cells are native cells that are not effectively suppressed by the immune system, and research has shown that it can be possible to engineer TCRs, antibodies, and other antigen-recognition molecules to target the cancer-specific MHC-peptide complexes on cancer cells. While targeted treatments with engineered antigen-recognition molecules may be effective to neutralize intended target cells, side effects of the treatment may be severe if engineered antigen-recognition molecules attack off-target native cells in addition to the intended target cells. Side effects are often identified during clinical trials, which can result in patient death, other adverse effects on patients, and expenditure of time and resources in research and development. Accordingly, there is a need in the art for methods and systems that allow for accurate and efficient prediction of off- targets to the target peptide of interest which helps evaluate the risk associated with the target peptide at the target selection step as well as help in screening the most specific antigen-recognition molecules. SUMMARY A workflow is presented herein which includes methods and computational systems and devices which are configured to execute computational steps of the methods. Computational systems and methods are presented herein for providing 3D computational models of potential off- target peptides each positioned in a groove of an MHC molecule (“MHC-off-target models”), quantifying structural similarity between each potential off-target peptide to a target peptide based on a comparison of the MHC-off-target models to a 3D computational model of a target MHC-Attorney Docket #: 250298.000961 peptide complex (“MHC-target model”), and ranking the potential off-target peptides based on a structural similarity metric. Examples are provided in which aspects of the methods and systems can be applied to solve bioinformatics and treatment development problems. One embodiment includes a method for providing one or more off-target 3D computational models of a potential off-target peptide in a groove of an MHC molecule (“comparison MHC-off-target models”) for comparison to a 3D computational model of a target peptide in a complex with the MHC molecule (“MHC-target model”). The method includes generating a coarse-grained model of the potential off-target peptide in the groove of the MHC molecule (“coarse-grained MHC-off-target model”) by a substituting, in the MHC-target model, an amino acid sequence of the potential off-target peptide in place of an amino acid sequence of the target peptide; generating a plurality of refined computational models of the potential off-target peptide in the groove of the MHC molecule (“refined MHC-off-target models”) by computationally optimizing the coarse-grained MHC-off-target model multiple times such that each optimization of the coarse-grained MHC-off-target model results in a respective refined MHC-off-target model of the plurality of refined MHC-off-target models; and selecting the one or more comparison MHC-off-target models from the plurality of refined MHC-off-target models such that the one or more comparison MHC-off-target models have lower energy than a majority of the plurality of the refined MHC-off-target models. One embodiment includes a method for quantifying structural similarity between a potential off-target peptide in a groove of an MHC molecule and a target peptide in complex with the MHC molecule for the purposes of antigen-recognition molecule binding. The method includes obtaining a plurality of 3D computational models of the potential off-target peptide in the groove of the MHC molecule (“comparison MHC-off-target models”); calculating, for each of the plurality of comparison MHC-off-target models, one or more structural similarity metrics such that each of the one or more structural similarity metrics comprises a corresponding value for each of the plurality of comparison MHC-off-target models and represents a measure of structural similarity between the comparison MHC-off-target model and a 3D computational model of the target peptide in complex with the MHC molecule (“MHC-target model”); and calculating, for each of the one or more structural similarity metrics, a single composite structural similarity metric comprising a value based at least in part on the corresponding structural similarity metric values for at least a portion of the plurality of comparison MHC-off-target models.Attorney Docket #: 250298.000961 One embodiment includes a method for identifying potential off-target peptide(s) based on sequence similarity and structural similarity for an antigen-recognition molecule that recognizes a target peptide presented in complex with an MHC molecule (MHC-target peptide complex. The method includes obtaining a pool of peptides of suitable length, optionally wherein the pool of peptides are expressed in normal tissues, optionally essential, normal tissues; identifying, within the pool, high sequence similarity peptides that have (i) more amino acid sequence similarity to the target peptide than a majority of peptides within the pool and (ii) have a binding affinity to the MHC molecule greater than a threshold value; and identifying the potential off-target peptides by selecting within the high sequence similarity peptides, the peptide(s) that are more structurally similar, when positioned in a groove of the MHC molecule, to the MHC-target peptide complex than a majority of the high sequence similarity peptides. One embodiment includes a method of ranking a plurality of potential off-target peptides of a target peptide. The method includes obtaining a 3D computational model of a target peptide in complex with the MHC molecule (“MHC-target model”); obtaining a plurality of off target 3D computational models of a potential off-target peptide in a groove of an MHC molecule (“comparison MHC-off-target models”) such that each of the plurality of off-target peptides is respectively represented in one or more comparison MHC-off-target models of the plurality of comparison MHC-off-target models; computing a structural similarly metric for each of the plurality of off-target peptides such that the structural similarity metric indicates a degree of similarity between the MHC-target model and at least a portion of the one or more comparison MHC-off-target models associated with the respective potential off-target peptide; and ranking the plurality of potential off-target peptides based at least in part on the structural similarity metric. One embodiment includes a for ranking potential target peptides to mitigate off-target toxicity. The method includes obtaining two or more potential target peptides among disease- associated peptides that are predicted to bind to an MHC molecule; obtaining, for each of the potential target peptides, a respective list of potential off-target peptides; ranking, for each of the potential target peptides, potential off-target peptides within the respective list of off-target peptides based at least in part on structural similarity of each potential off-target peptide to the potential target peptide; and ranking the two or more potential target peptides based at least in part on the ranking of potential off-target peptides within the respective list of potential off-target peptides.Attorney Docket #: 250298.000961 One embodiment includes a method of ranking a plurality of potential off-target peptides for a target peptide. The method includes providing a target conformation, wherein the target conformation is a computational representation of a three-dimensional structure comprising the target peptide and a groove of a major histocompatibility complex (MHC) molecule, wherein the target peptide is positioned within the groove for binding to the MHC molecule; providing a plurality of off-target conformations, wherein each off-target conformation is a computational representation of a three-dimensional structure comprising a potential off-target peptide and the groove of the MHC molecule and wherein each of the off-target conformations corresponds to one of the plurality of potential off-target peptides positioned within the groove for binding to the MHC molecule; aligning the target conformation with each of the off-target conformations in three- dimensional space; computing a difference value for each of the off-target conformations, wherein each difference value quantifies a difference between the target conformation and one of the off- target conformations; and ranking the plurality of off-target conformations based on their respective difference values. One embodiment includes a non-transitory computer-readable medium configured to communicate with one or more processor(s) of a computational device, the non-transitory computer-readable medium including instructions thereon, that when executed by the processor(s), cause the computational device to perform any of the methods described herein. Steps of the method embodiments can be executed in various orders to achieve the desired output of the method as understood by a person skilled in the pertinent art. Methods can include additional and / or alternative steps as understood by a person skilled in the pertinent art. One embodiment includes a system of one or more computers configured to perform particular operations or actions by virtue of having software, firmware, hardware, or a combination of them installed on the system that in operation causes or cause the system to perform the actions. One or more computer programs can be configured to perform particular operations or actions by virtue of including instructions that, when executed by data processing apparatus, cause the apparatus to perform the actions. The system of one or more computers can be configured to computationally carry out at least a portion of the steps of some or all of the method embodiments. For instance, the system can include non-transitory computer-readable medium in communication with one or more processors, and including instructions thereon, that when executed by the processor(s) causes the system to execute steps of the method embodiments.Attorney Docket #: 250298.000961 BRIEF DESCRIPTION OF THE DRAWINGS The above and further aspects of this invention should be read with reference to the drawings, in which like elements in different drawings are identically numbered. The drawings, which are not necessarily to scale, depict selected embodiments and are not intended to limit the scope of the invention. The detailed description illustrates by way of example, not by way of limitation, the principles of the invention. This description will clearly enable one skilled in the art to make and use the invention, and describes several embodiments, adaptations, variations, alternatives, and uses of the invention, including what is presently believed to be the best mode of carrying out the invention. The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication with color drawings will be provided by the Office upon request and payment of the necessary fee. FIG. 1 is a flow diagram illustrating an exemplary method for ranking a plurality of potential off-target peptides of a target peptide. FIG. 2 is a flow diagram illustrating an exemplary method for providing one or more comparison MHC-off-target models for comparison to an MHC-target model. FIG. 3 is a flow diagram illustrating an exemplary method for quantifying structural similarity between a potential off-target peptide in a groove of an MHC molecule and a target peptide in complex with the MHC molecule for the purposes of antigen-recognition molecule binding. FIG. 4 is a flow diagram illustrating an exemplary method for identifying potential off- target peptide(s) based on sequence similarity and structural similarity for an antigen-recognition molecule that recognizes a target peptide presented in complex with an MHC molecule (MHC- target peptide complex). FIG. 5 is a flow diagram illustrating an exemplary method for ranking potential target peptides to mitigate off-target toxicity. FIG. 6 is a block diagram of an exemplary system for development of an antigen recognition molecule. FIG. 7 is a block diagram of an exemplary structure-based off-target prediction engine. FIG. 8 is a block diagram of an embodiment of the structure-based off-target prediction engine.Attorney Docket #: 250298.000961 FIG. 9 is a block diagram of another embodiment of the structure-based off-target prediction engine. FIG. 10 illustrates a block diagram of an exemplary embodiment of a target toxicity database. FIG. 11 illustrates a block diagram of an embodiment of a computing device. FIG. 12 illustrates a block diagram of an embodiment of a computing network. FIG. 13 illustrates cellular functions related to the example embodiments presented herein. FIG. 14 is a block diagram of an embodiment of the structure-based off-target prediction engine applied as a proof of concept to a MAGEA3168-176 (EVDPIGHLY (SEQ ID NO: 29)) – HLA- A*01:01 complex. FIG. 15 is a block diagram of another embodiment of the structure-based off-target prediction engine applied as a proof of concept to a MAGEA3168-176 (EVDPIGHLY (SEQ ID NO: 29)) – HLA-A*01:01 complex. FIGs. 16A through 16E include a chart in which 231 potential off-target peptides of the MAGEA3168-176 (EVDPIGHLY (SEQ ID NO: 29)) – HLA-A*01:01 complex are ranked according to root mean square deviation (RMSD) of conformation of the respective off-target peptide to the target peptide. FIG. 16A includes the top 50 off-target peptides, i.e., highest priority, highest ranked off-target peptides. FIG.16A discloses SEQ ID NOS 202-207, 47, 208-214, 216-219, 215, 220-230, 45, 261-266, 232, and 267-278, respectively, in order of appearance. FIG. 16B includes the 51stthrough 100thranked off-target peptides. FIG. 16B discloses SEQ ID NOS 279-324, 39, and 325-327, respectively, in order of appearance. FIG. 16C includes the 101stthrough 150thranked off-target peptides. FIG.16C discloses SEQ ID NOS 328-339, 44, 340-352, 231, 353-368, 32, 369, 41, and 370-373, respectively, in order of appearance. FIG. 16D includes the 151stthrough 200thranked off-target peptides. FIG. 16D discloses SEQ ID NOS 374-392, 43, 393-418, 30, and 419-421, respectively, in order of appearance. FIG. 16E includes the 201stthrough 231stranked off-target peptides. FIG. 16E discloses SEQ ID NOS 422-437, 31, and 438-451, respectively, in order of appearance. FIGs. 17A through 17E include a chart in which 231 potential off-target peptides of the MAGEA3168-176 (EVDPIGHLY (SEQ ID NO: 29)) – HLA-A*01:01 complex are ranked according to root mean square deviation (RMSD) of conformation of the respective off-target peptide andAttorney Docket #: 250298.000961 HLA groove to the target HLA-peptide complex. FIG.17A includes the top 50 off-target peptides, i.e., highest priority, highest ranked off-target peptides. FIG. 17A discloses SEQ ID NOS 47, 45, 209, 231-232, 321, 39, 218, 215, 217, 368, 313, 281, 263, 431, 269, 443, 452, 294, 314, 207, 361, 346, 283, 223, 227, 279, 204, 332, 406, 342, 213, 261, 367, 325, 324, 229, 203, 326, 339, 369, 208, 374, 340, 320, 216, 211, 319, 268, and 225, respectively, in order of appearance. FIG. 17B includes the 51stthrough 100thranked off-target peptides. FIG. 17B discloses SEQ ID NOS 262, 205, 311, 376, 286, 214, 438, 206, 301, 389, 344, 222, 296, 380, 219, 32, 271, 212, 440, 336, 333, 322, 210, 221, 273, 266, 354, 416, 226, 338, 270, 295, 299, 364, 435, 427, 419, 312, 334, 350, 335, 317, 331, 228, 377, 407, 297, 359, 292, and 449, respectively, in order of appearance. FIG. 17C includes the 101stthrough 150thranked off-target peptides. FIG. 17C discloses SEQ ID NOS 363, 293, 396, 316, 291, 351, 373, 399, 43, 309, 308, 372, 337, 304, 274, 362, 387, 224, 403, 415, 202, 392, 288, 352, 30, 451, 328, 421, 285, 381, 408, 298, 425, 353, 386, 409, 400, 275, 341, 422, 414, 277, 300, 411, 441, 429, 410, 357, 358, and 437, respectively, in order of appearance. FIG. 17D includes the 151stthrough 200thranked off-target peptides. FIG. 17D discloses SEQ ID NOS 404, 379, 278, 315, 306, 398, 397, 302, 402, 264, 453, 375, 318, 230, 284, 282, 307, 329, 370, 347, 428, 348, 417, 310, 265, 436, 276, 378, 395, 267, 433, 442, 401, 323, 413, 280, 394, 366, 220, 371, 305, 349, 287, 360, 384, 289, 450, 44, 365, and 343, respectively, in order of appearance. FIG. 17E includes the 201stthrough 231stranked off-target peptides. FIG. 17E discloses SEQ ID NOS 430, 303, 426, 423, 41, 424, 432, 393, 439, 418, 444, 355, 446, 390, 290, 356, 383, 412, 385, 388, 272, 330, 420, 345, 31, 405, 448, 327, 391, 445, and 447, respectively, in order of appearance. FIGs. 18A through 18E include a chart in which 231 potential off-target peptides of the MAGEA3168-176(EVDPIGHLY (SEQ ID NO: 29)) – HLA-A*01:01 complex are ranked according to similarity of molecular surface interaction fingerprints (MSIFs) of the respective off-target peptide and HLA groove to the target HLA-peptide complex. FIG. 18A includes the top 50 off- target peptides, i.e., highest priority, highest ranked off-target peptides. FIG. 18A discloses SEQ ID NOS 311, 419, 292, 452, 359, 318, 229, 209, 47, 269, 43, 223, 232, 357, 44, 393, 399, 447, 309, 387, 317, 203, 424, 306, 453, 215, 383, 261, 320, 421, 380, 427, 301, 308, 414, 362, 406, 281, 325, 369, 270, 213, 290, 342, 454, 202, 341, 287, 265, and 207, respectively, in order of appearance. FIG. 18B includes the 51stthrough 100thranked off-target peptides. FIG. 18B discloses SEQ ID NOS 206, 347, 397, 413, 355, 30, 435, 405, 450, 381, 319, 339, 312, 299, 219, 214, 221, 327, 295, 375, 263, 332, 222, 402, 288, 417, 390, 204, 225, 230, 389, 358, 321, 386,Attorney Docket #: 250298.000961 337, 374, 330, 437, 368, 348, 227, 446, 45, 267, 403, 316, 216, 336, 277, and 338, respectively, in order of appearance. FIG. 18C includes the 101stthrough 150thranked off-target peptides. FIG. 18C discloses SEQ ID NOS 326, 291, 212, 268, 224, 226, 443, 367, 39, 377, 329, 324, 379, 353, 401, 363, 211, 378, 400, 231, 266, 384, 278, 433, 279, 310, 360, 280, 349, 286, 428, 333, 31, 404, 334, 425, 407, 373, 442, 217, 305, 345, 307, 432, 303, 208, 285, 429, 356, and 282, respectively, in order of appearance. FIG.18D includes the 151stthrough 200thranked off-target peptides. FIG. 18D discloses SEQ ID NOS 436, 409, 351, 331, 340, 364, 323, 431, 395, 366, 408, 272, 296, 275, 274, 293, 361, 398, 262, 376, 372, 346, 300, 273, 370, 297, 411, 322, 220, 394, 276, 392, 371, 304, 388, 422, 210, 426, 445, 412, 448, 264, 396, 41, 328, 314, 441, 423, 410, and 343, respectively, in order of appearance. FIG. 18E includes the 201stthrough 231stranked off-target peptides. FIG. 18E discloses SEQ ID NOS 294, 271, 335, 420, 350, 391, 438, 283, 354, 315, 289, 218, 344, 32, 416, 298, 444, 451, 418, 415, 313, 430, 449, 385, 228, 302, 205, 284, 352, 440, and 439, respectively, in order of appearance. FIG. 18F discloses SEQ ID NOS 311, 419, 292, 452, 359, 318, 229, 209, 47 and 269, respectively, in order of appearance. FIG. 19A illustrates a superposition of a 3D computational model of the MAGEA3168-176(EVDPIGHLY (SEQ ID NO: 29)) in a complex with the HLA-A*01:01 MHC molecule and a 3D computational model of the TTN off-target peptide ESDPIVAQY (SEQ ID NO: 47) in the groove of the HLA-A*01:01 molecule. FIG. 19B illustrates a superposition of a 3D computational model of the TTN off-target peptide ESDPIVAQY (SEQ ID NO: 47) in the groove of the HLA-A*01:01 molecule and an experimentally determined 3D computational model of the TTN off-target peptide ESDPIVAQY (SEQ ID NO: 47) in the groove of the HLA-A*01:01 molecule for the sake of verifying the exemplary methods illustrated in FIGs. 14 and 15. FIG. 20A illustrates a superposition of a 3D computational model of the MAGEA3168-176(EVDPIGHLY (SEQ ID NO: 29)) in a complex with the HLA-A*01:01 MHC molecule and a 3D computational model of the MRPL43 potential off-target peptide TVDPISSSL (SEQ ID NO: 202) in the groove of the HLA-A*01:01 molecule. FIG. 20B illustrates a superposition of a 3D computational model of the MAGEA3168-176(EVDPIGHLY (SEQ ID NO: 29)) in a complex with the HLA-A*01:01 MHC molecule and a 3D computational model of the IGHM off-target peptide ESATITCLV (SEQ ID NO: 204) in the groove of the HLA-A*01:01 molecule.Attorney Docket #: 250298.000961 FIG. 21 is a block diagram of an embodiment of the structure-based off-target prediction engine applied as a proof of concept to a WT1126- 134RMFPNAPYL (SEQ ID NO: 241) – HLA- A*02:01 complex. FIGs. 22A through 22D include a chart in which 142 potential off-target peptides of the WT1126- 134RMFPNAPYL (SEQ ID NO: 241) – HLA-A*02:01 complex are ranked according to root mean square deviation (RMSD) of conformation of the respective off-target peptide to the target. FIG. 22A includes the top 40 off-target peptides, i.e., highest priority, highest ranked off- target peptides. FIG.22A discloses SEQ ID NOS 455-457, 235, 238, 458-463, 237, 464, 240, 465- 467, 233, and 468-489, respectively, in order of appearance. FIG. 22B includes the 41stthrough 80thranked off-target peptides. FIG. 22B discloses SEQ ID NOS 490-503, 239, and 504-528, respectively, in order of appearance. FIG. 22C includes the 81stthrough 120thranked off-target peptides. FIG. 22C discloses SEQ ID NOS 529-549, 236, and 550-567, respectively, in order of appearance. FIG. 22D includes the 121stthrough 142ndranked off-target peptides. FIG. 22D discloses SEQ ID NOS 568-586 and 249-251, respectively, in order of appearance. FIGs. 23A through 23D include a chart in which 142 potential off-target peptides of the WT1126- 134 RMFPNAPYL (SEQ ID NO: 241) – HLA-A*02:01 complex are ranked according to root mean square deviation (RMSD) of conformation of the respective off-target peptide to the target at residue positions 1, 2, 3, and 4 only. FIG. 23A includes the top 40 off-target peptides, i.e., highest priority, highest ranked off-target peptides. FIG. 23A discloses SEQ ID NOS 488, 505, 457, 237, 552, 504, 578, 570, 528, 482, 463, 553, 235, 238, 455, 495, 456, 236, 240, 233, 467, 479, 500, 459, 501, 466, 525, 522, 511, 506, 516, 518, 503, 567, 475, 458, 476, 531, 513, and 470, respectively, in order of appearance. FIG.23B includes the 41stthrough 80thranked off-target peptides. FIG. 23B discloses SEQ ID NOS 535, 494, 461, 468, 559, 496, 558, 557, 460, 524, 462, 478, 473, 489, 465, 464, 491, 477, 481, 517, 472, 469, 498, 471, 573, 530, 583, 521, 250, 249, 586, 561, 581, 541, 508, 572, 585, 502, 251, and 564, respectively, in order of appearance. FIG. 23C includes the 81stthrough 120thranked off-target peptides. FIG. 23C discloses SEQ ID NOS 239, 580, 515, 538, 512, 520, 497, 551, 532, 523, 534, 487, 545, 499, 529, 484, 582, 542, 574, 483, 568, 480, 509, 533, 550, 526, 566, 560, 555, 577, 543, 527, 576, 569, 507, 565, 474, 563, 575, and 584, respectively, in order of appearance. FIG. 23D includes the 121stthrough 142ndranked off-target peptides. FIG. 23D discloses SEQ ID NOS 490, 493, 519, 547, 485, 546, 549,Attorney Docket #: 250298.000961 514, 571, 537, 486, 562, 492, 510, 536, 556, 544, 554, 579, 548, and 539-540, respectively, in order of appearance. FIG. 24A illustrates a superposition of a 3D computational model of the WT1126-134 RMFPNAPYL (SEQ ID NO: 241) target peptide in a complex with the HLA-A*02:01 MHC molecule and a 3D computational model of the SF3B4 off-target peptide KLYGKPIRV (SEQ ID NO: 235) in the groove of the HLA-A*02:01 molecule. FIG. 24B illustrates a superposition of a 3D computational model of the WT1126-134 RMFPNAPYL (SEQ ID NO: 241) target peptide in a complex with the HLA-A*02:01 MHC molecule and a 3D computational model of the ILF2 off-target peptide KILPTLEAV (SEQ ID NO: 233) in the groove of the HLA-A*02:01 molecule. FIG. 24C illustrates a superposition of a 3D computational model of the WT1126-134RMFPNAPYL (SEQ ID NO: 241) target peptide in a complex with the HLA-A*02:01 MHC molecule and a 3D computational model of the USP9Y off-target peptide RLWGEPVNL (SEQ ID NO: 240) in the groove of the HLA-A*02:01 molecule. FIG. 24D illustrates a superposition of a 3D computational model of the WT1126-134RMFPNAPYL (SEQ ID NO: 241) target peptide in a complex with the HLA-A*02:01 MHC molecule and a 3D computational model of the SHC1 off-target peptide RVPPPPQSV (SEQ ID NO: 236) in the groove of the HLA-A*02:01 molecule. FIG. 25A illustrates an X-Ray structure of ESK in complex with HLA-A*02:01 / WT1126- 134. FIG. 25A discloses SEQ ID NO: 241. FIG.25B illustrates the X-Ray structure of ESK in complex with HLA-A*02:01 / WT1126-134of FIG. 25A with a 3D computational model of off-target peptide KLYGKPIRV (SEQ ID NO: 235) in the groove of the HLA-A*02:01 molecule. FIG.25B discloses SEQ ID NOS 241 and 235, respectively, in order of appearance. DEFINITIONS Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one skilled in the pertinent art. Singular forms “a”, “an”, and “the” include plural references unless the context clearly dictates otherwise. Thus, for example, a reference to “a method” includes one or more methods,Attorney Docket #: 250298.000961 and / or steps of the type described herein and / or which will become apparent to those persons skilled in the art upon reading this disclosure. The term “about” or “approximately” includes being within a meaningful range of a value. The allowable variation encompassed by the term “about” or “approximately” depends on the particular system under study, and can be readily appreciated by one skilled in the pertinent art. The terms “major histocompatibility complex,” and “MHC” encompass the terms “human leukocyte antigen” or “HLA” (the latter two of which are generally reserved for human MHC molecules), naturally occurring MHC molecules (e.g., MHC class I molecule comprising MHC class I α (heavy) chain and β2 microglobulin; MHC class II molecule comprising MHC class II α chain and MHC class II β chain), individual chains of MHC molecules (e.g., MHC class I α (heavy) chain, MHC class II α chain, and MHC class II β chain), individual subunits of such chains of MHC molecules (e.g., α1, α2, and / or α3 subunits of MHC class I α chain, α1-α2 subunits of MHC class II α chain, β1-β2 subunits of MHC class II β chain) as well as portions (e.g., the peptide-binding portions, e.g., the peptide-binding grooves), mutants and various derivatives thereof (including fusions proteins), wherein such portion, mutants and derivatives retain the ability to display an antigenic peptide for recognition by a T-cell receptor (TCR), e.g., an antigen- specific TCR. An MHC class I molecule comprises a peptide binding groove formed by the α1 and α2 domains of the heavy a chain that can stow a peptide of around 14 amino acids. In certain embodiments, an MHC class I molecule can stow a peptide of about 8 amino acids in length. In certain embodiments, an MHC class I molecule can stow a peptide of about 9 amino acids in length. In certain embodiments, an MHC class I molecule can stow a peptide of about 10 amino acids in length. In certain embodiments, an MHC class I molecule can stow a peptide of about 11 amino acids in length. In certain embodiments, an MHC class I molecule can stow a peptide of about 12 amino acids in length. In certain embodiments, an MHC class I molecule can stow a peptide of about 13 amino acids in length. In certain embodiments, an MHC class I molecule can stow a peptide of about 14 amino acids in length. Despite the fact that both classes of MHC bind a core of about 9 amino acids (e.g., 5 to 16 amino acids) within peptides, the open-ended nature of MHC class II peptide binding groove (the α1 domain of a class II MHC α polypeptide in association with the β1 domain of a class II MHC β polypeptide) allows for a wider range of peptide lengths. Peptides binding MHC class II usually vary between 12 and 20 amino acids inAttorney Docket #: 250298.000961 length, though shorter or longer lengths (e.g., 23 amino acids in length) are not uncommon. As a result, peptides may shift within the MHC class II peptide binding groove, changing which 9-mer sits directly within the groove at any given time. In certain embodiments, an MHC class II molecule can stow a peptide of about 12 amino acids in length. In certain embodiments, an MHC class II molecule can stow a peptide of about 13 amino acids in length. In certain embodiments, an MHC class II molecule can stow a peptide of about 14 amino acids in length. In certain embodiments, an MHC class II molecule can stow a peptide of about 15 amino acids in length. In certain embodiments, an MHC class II molecule can stow a peptide of about 16 amino acids in length. In certain embodiments, an MHC class II molecule can stow a peptide of about 17 amino acids in length. In certain embodiments, an MHC class II molecule can stow a peptide of about 18 amino acids in length. In certain embodiments, an MHC class II molecule can stow a peptide of about 19 amino acids in length. In certain embodiments, an MHC class II molecule can stow a peptide of about 20 amino acids in length. In some embodiments, the MHC-peptide complex described herein may be an MHC-peptide complex from a non-human animal. In other embodiments, the MHC-peptide complex described herein may include an HLA-peptide complex, i.e., an MHC-peptide complex from a human. The term “non-human animal” and the like refers to any vertebrate organism that is not a human. In some embodiments, a non-human animal is a cyclostome, a bony fish, a cartilaginous fish (e.g., a shark or a ray), an amphibian, a reptile, a mammal, and a bird. In some embodiments, a non-human animal is a mammal. In some embodiments, a non-human mammal is a primate, a goat, a sheep, a pig, a dog, a cow, or a rodent. In some embodiments, a non-human animal is a rodent such as a rat or a mouse. The term “antigen” refers to any agent (e.g., protein, peptide, polysaccharide, glycoprotein, glycolipid, nucleotide, portions thereof, or combinations thereof) that, when introduced into an immunocompetent host is recognized by the immune system of the host and elicits an immune response by the host. The T-cell receptor recognizes a peptide presented in the context of a major histocompatibility complex (MHC) as part of an immunological synapse. The peptide-MHC (pMHC) complex is recognized by TCR, with the peptide (antigenic determinant) and the TCR idiotype providing the specificity of the interaction. Accordingly, the term “antigen” encompasses peptides presented in the context of MHCs, e.g., peptide-MHC complexes. The peptide displayed on MHC may also be referred to as an “epitope” or an “antigenic determinant”.Attorney Docket #: 250298.000961 The terms “peptide,” “antigenic determinant,” “epitopes,” etc., encompass not only those presented naturally by antigen-presenting cells (APCs), but may be any desired peptide so long as it is recognized by an immune cell of an animal, e.g., when presented appropriately to the cells of an immune system. For example, a peptide having an artificially prepared amino acid sequence may also be used as the epitope. The term “antigen-recognition molecule” refers to any molecule that is capable of recognizing an antigen as defined above. Antigen-recognition molecules can include, but are not limited to, T cell receptors (TCR), antibodies, antibody fragments, or chimeric antigen receptors (CARs). “MHC-peptide complex,” “peptide-MHC complex,” “pMHC complex,” “peptide-in- groove,” and the like includes: (i) an MHC molecule, e.g., a human and / or non-human animal MHC molecule, or portion thereof (e.g., the peptide-binding groove thereof, and e.g., the extracellular portion thereof), and (ii) a peptide (e.g., an antigenic peptide), where the MHC molecule and the peptide are complexed in such a manner that the pMHC complex can specifically bind a T-cell receptor. A pMHC complex encompasses cell surface expressed pMHC complexes and soluble pMHC complexes. “HLA-peptide complex,” “peptide-HLA complex,” “pHLA complex,” and the like refers to an MHC-peptide complex wherein the MHC molecule is a Human Leukocyte Antigen (HLA) molecule. The terms “antibody,” “antibodies,” “immunoglobulin, “binding protein” and the like refer to monoclonal antibodies, multispecific antibodies, human antibodies, humanized antibodies, chimeric antibodies, single-chain Fvs (scFv), single chain antibodies, Fab fragments, F(ab′) fragments, disulfide-linked Fvs (sdFv), intrabodies, minibodies, diabodies and anti-idiotypic (anti- Id) antibodies (including, e.g., anti-Id antibodies to antigen-specific TCR), and epitope-binding fragments of any of the above. The terms “antibody” and “antibodies” also refer to covalent diabodies such as those disclosed in U.S. Pat. Appl. Pub. 20070004909, incorporated herein by reference in its entirety, and Ig-DARTS such as those disclosed in U.S. Pat. Appl. Pub. 20090060910, incorporated herein by reference in its entirety. In some instances, an immunoglobulin or antibody may be a membrane-bound immunoglobulin or antibody, such as a B Cell Receptor (BCR).Attorney Docket #: 250298.000961 A “pMHC-binding protein” refers to an antigen-binding protein (e.g., an immunoglobulin, antibody, TCR, CAR, or the like) that specifically binds a pMHC complex. An “individual” or “subject” or “animal” refers to humans, veterinary animals (e.g., cats, dogs, cows, horses, sheep, pigs, etc.) and experimental animal models of diseases (e.g., mice, rats). In one embodiment, the subject is a human. The terms “protein” and “polypeptide”, used interchangeably herein, encompass all kinds of naturally occurring and synthetic proteins, including protein fragments of all lengths, fusion proteins and modified proteins, including without limitation, glycoproteins, as well as all other types of modified proteins (e.g., proteins resulting from phosphorylation, acetylation, myristoylation, palmitoylation, glycosylation, oxidation, formylation, amidation, polyglutamylation, ADP-ribosylation, pegylation, biotinylation, etc.). Small polypeptides of less than 100 amino acids, preferably less than 50 amino acids, may be referred to as “peptides”. The terms “polynucleotide” and “nucleic acid”, used interchangeably herein, include polymeric forms of nucleotides of any length, including ribonucleotides (RNA), deoxyribonucleotides (DNA), or analogs or modified versions thereof. They include single-, double-, and multi-stranded DNA or RNA, genomic DNA, complementary DNA (cDNA), DNA- RNA hybrids, and polymers comprising purine bases, pyrimidine bases, or other natural, chemically modified, biochemically modified, non-natural, or derivatized nucleotide bases. In general, a "promoter" or "promoter sequence" is a DNA regulatory region capable of binding an RNA polymerase in a cell (e.g., directly or through other promoter-bound proteins or substances) and initiating transcription of a coding sequence. A promoter may be operably linked to other expression control sequences, including enhancer and repressor sequences and / or with a polynucleotide described herein. The term “operably linked” or the like refers to a juxtaposition wherein the components described are in a relationship permitting them to function in their intended manner. For example, a control sequence “operably linked” to a coding sequence is ligated in such a way that expression of the coding sequence is achieved under conditions compatible with the control sequences. “Operably linked” sequences include both expression control sequences that are contiguous with a gene of interest and expression control sequences that act in trans or at a distance to control a gene of interest (or sequence of interest). The term “expression control sequence” includes polynucleotide sequences, which are necessary to affect the expression and processing of codingAttorney Docket #: 250298.000961 sequences to which they are ligated. “Expression control sequences” include: appropriate transcription initiation, termination, promoter and enhancer sequences; efficient RNA processing signals such as splicing and polyadenylation signals; sequences that stabilize cytoplasmic mRNA; sequences that enhance translation efficiency (i.e., Kozak consensus sequence); sequences that enhance polypeptide stability; and when desired, sequences that enhance polypeptide secretion. The nature of such control sequences differs depending upon the host organism. For example, in prokaryotes, such control sequences generally include promoters, ribosomal binding sites and transcription termination sequences, while in eukaryotes typically such control sequences include promoters and transcription termination sequences. The term “control sequences” is intended to include components whose presence is essential for expression and processing, and can also include additional components whose presence is advantageous, for example, leader sequences and fusion partner sequences. The term “isolated” refers to a homogenous population of molecules (such as polynucleotides or polypeptides) which have been substantially separated and / or purified away from other components of the system the molecules are produced in, such as a recombinant cell, as well as a protein that has been subjected to at least one purification or isolation step. In certain aspects, “isolated” refers to a molecule that is substantially free of other cellular material and / or chemicals and encompasses molecules that are isolated to a higher purity, such as to 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% purity. The term “isolated” as used herein may also refer to a cell, or homogenous population of cells, that has been removed from its natural environment and substantially separated from other cellular components with which it is naturally associated. This includes cells that have been cultured in vitro or otherwise manipulated outside of their native biological context. The term encompasses cells that are part of a purified population, free from significant contamination by other cell types, and may include, e.g., genetically modified cells, stem cells, or cells derived from tissues or organs. In some embodiments, an isolated cell of the present disclosure is an immune cell, e.g., an antigen-presenting cell (APC).. The term “derivative” as used herein refers to a peptide, polypeptide, or polynucleotide, or a variant or analog thereof, comprising one or more mutations and / or chemical modifications as compared to a reference peptide, polypeptide or polynucleotide. Mutations and / or chemical modifications are further detailed below and can include, for example, insertions, substitutions,Attorney Docket #: 250298.000961 deletions, transversions, and / or inversions at one or more locations in the amino acid or nucleotide sequence. The term “library” refers to an isolated collection of at least two elements that differ from one another in at least one aspect. For example, a “peptide library” is a collection of at least two peptides that may differ from one another by at least one amino acid. As another example, a “pMHC complex library” is a collection of pMHC complexes that may differ from one another by at least one amino acid in the peptide or at least one MHC polypeptide. The elements of the library are isolated from like type of elements that are not part of the library (e.g., peptides of a peptide library are isolated from peptides that are not part of the library). The library may exist in vitro or ex vivo. One or more elements (e.g., each element) of the library may be isolated from one or more other elements (e.g., each other element) of the library. A library may be “sorted” such that each of the one or more isolated elements exists in an identifiable and accessible physical space, such as a cell or a container, so that each set of the one or more isolated elements may be selectively accessed or pulled from the library for use according to the disclosure elsewhere herein. Each container may be separable (e.g., a vial) or part of an integral solid support (e.g., an individual well of a multi-well plate). One or more elements of a library (including partial portions or the entirety of the library) may be used according to the disclosure herein. Various elements of a library may be used contemporaneously or consecutively, such as for screening antigen-recognition molecules for off-target cross-reactivity. In accordance with the disclosure herein, there may be employed conventional molecular biology, microbiology, and recombinant DNA techniques within the skill of the art. Such techniques are explained fully in the literature. See, e.g., Sambrook, Fritsch & Maniatis, Molecular Cloning: A Laboratory Manual, Second Edition. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 1989 (herein “Sambrook et al., 1989”); DNA Cloning: A Practical Approach, Volumes I and II (D.N. Glover ed.1985); Oligonucleotide Synthesis (M.J. Gait ed.1984); Nucleic Acid Hybridization [B.D. Hames & S.J. Higgins eds. (1985)]; Transcription And Translation [B.D. Hames & S.J. Higgins, eds. (1984)]; Animal Cell Culture [R.I. Freshney, ed. (1986)]; Immobilized Cells And Enzymes [IRL Press, (1986)]; B. Perbal, A Practical Guide To Molecular Cloning (1984); Ausubel, F.M. et al. (eds.). Current Protocols in Molecular Biology. John Wiley & Sons, Inc., 1994. These techniques include site directed mutagenesis as described in Kunkel, Proc. Natl. Acad. Sci. USA 82: 488- 492 (1985), U. S. Patent No. 5,071, 743, Fukuoka et al., Biochem.Attorney Docket #: 250298.000961 Biophys. Res. Commun. 263: 357-360 (1999); Kim and Maas, BioTech. 28: 196-198 (2000); Parikh and Guengerich, BioTech. 24: 428-431 (1998); Ray and Nickoloff, BioTech. 13: 342-346 (1992); Wang et al., BioTech. 19: 556-559 (1995); Wang and Malcolm, BioTech. 26: 680-682 (1999); Xu and Gong, BioTech.26: 639-641 (1999), U.S. Patents Nos.5,789, 166 and 5,932, 419, Hogrefe, Strategies l4. 3: 74-75 (2001), U. S. Patents Nos. 5,702,931, 5,780,270, and 6,242,222, Angag and Schutz, Biotech. 30: 486-488 (2001), Wang and Wilkinson, Biotech. 29: 976-978 (2000), Kang et al., Biotech.20: 44-46 (1996), Ogel and McPherson, Protein Engineer.5: 467-468 (1992), Kirsch and Joly, Nucl. Acids. Res.26: 1848-1850 (1998), Rhem and Hancock, J. Bacteriol. 178: 3346-3349 (1996), Boles and Miogsa, Curr. Genet. 28: 197-198 (1995), Barrenttino et al., Nuc. Acids. Res. 22: 541-542 (1993), Tessier and Thomas, Meths. Molec. Biol. 57: 229-237, and Pons et al., Meth. Molec. Biol. 67: 209-218. The term “administration” and the like refers to and includes the administration of a composition (e.g., antigen-recognition molecule) to a subject or system (e.g., to a cell, organ, tissue, organism, or relevant component or set of components thereof). The skilled artisan will appreciate that route of administration may vary depending, for example, on the subject or system to which the composition is being administered, the nature of the composition, the purpose of the administration, etc. For example, in certain embodiments, administration to an animal subject (e.g., to a human or a rodent) may be bronchial (including by bronchial instillation), buccal, enteral, interdermal, intra-arterial, intradermal, intragastric, intramedullary, intramuscular, intranasal, intraperitoneal, intrathecal, intravenous, intraventricular, mucosal, nasal, oral, rectal, subcutaneous, sublingual, topical, tracheal (including by intratracheal instillation), transdermal, vaginal and / or vitreal. In some embodiments, administration may involve intermittent dosing. In some embodiments, administration may involve continuous dosing (e.g., perfusion) for at least a selected period of time. The term “essential, normal tissues” refers to tissues of a patient where an activity of a given antigen-recognition molecule administered for treating a disease may create unacceptable side-effects. The list of tissues considered essential, normal would vary depending on the disease being treated and on the risks associated with the disease itself (e.g., the list would be smaller for life-threatening diseases than for non-life-threatening diseases). For example but not by way of limitation, when treating life-threatening cancers, tissue types that may be considered non-essential may include breast, ovary and testes. The list of tissues considered essential, normal would alsoAttorney Docket #: 250298.000961 vary depending on the likelihood for a given antigen-recognition molecule to reach such tissues. For example, brain may not be included in the list of essential, normal tissues in cases of antigen- recognition molecules which do not permeate blood-brain-barrier of patients with the disease being treated. The terms “component,” “engine,” “module,” “system,” “server,” “processor,” “memory,” and the like are intended to include one or more computer-related units, such as but not limited to hardware, firmware, a combination of hardware and software, software, or software in execution. For example, a component may be, but is not limited to being, a process running on a processor, an object, an executable, a thread of execution, a program, and / or a computer. By way of illustration, both an application running on a computing device and the computing device can be a component. One or more components can reside within a process and / or thread of execution and a component may be localized on one computer and / or distributed between two or more computers. In addition, these components can execute from various computer readable media having various data structures stored thereon. The components may communicate by way of local and / or remote processes such as in accordance with a signal having one or more data packets, such as data from one component interacting with another component in a local system, distributed system, and / or across a network such as the Internet with other systems by way of the signal. The term “3D computational model” refers to a computer-readable representation of a 3D (three-dimensional) structure that includes information about portions of the 3D structure in relation to each other. In examples presented herein in which the 3D structure includes one or more molecules, the 3D computational model of that 3D structure includes positions of atoms, or collections of atoms, in relation to each other. In some examples, the 3D computational model represents a conformation of molecule(s) such that arrangement in space of constituent atoms of the molecule(s) are represented in the 3D computational model. In examples presented herein in which the 3D structure includes a peptide, the 3D computational model includes positions of at least a portion of the amino acids of the peptide in relation to each other. For instance, a 3D computational model of a peptide may represent a conformation of the peptide, or a folded 3D structure of the peptide. For instance, a 3D computational model of a peptide, MHC molecule, and / or other molecule may be a file in Protein Data Bank (PDB) format, Macromolecular Crystallographic Information File (mmCIF or PDBx / mmCIF) format, Polygon File Format orAttorney Docket #: 250298.000961 Stanford Triangle Format (PLY), or other suitable file or data structure format as understood by a person skilled in the pertinent art. A 3D computational model of a peptide, a peptide in a groove of an MHC molecule, or a peptide in complex with an MHC molecule can be computationally generated, computationally refined, and / or based on experimentally determined structures. The terms “MHC-target model” and “MHC-off-target model” refer to 3D computational models of peptides positioned in the grooves of, or in complex with, MHC molecules, respectively a target peptide positioned in a groove of, or in complex with, an MHC molecule and an off-target peptide positioned in a groove of, or in complex with, an MHC molecule. For purposes of 3D computational models, a peptide may be considered to be positioned in the groove of an MHC molecule or in complex with an MHC molecule when positioned or docked in a conformation and orientation relative to the binding groove of the MHC molecule that optimizes, based on at least one measure, the probability of peptide binding or loading on to the MHC molecule, regardless of whether stable peptide binding / loading has been experimentally validated or does in fact occur. A given target peptide may be represented by one or more MHC-target models, and likewise a given off-target peptide may be represented by one or more MHC-target models. MHC-target models and MHC-off-target models can be generated computationally and / or based on experimentally determined structures. For instance, MHC-target models and MHC-off-target models can be experimentally determined using methods such as X-ray crystallography, cryogenic electron microscopy (cryo-EM), Nuclear Magnetic Resonance (NMR), other suitable experimental method as understood by a person skilled in the pertinent art, or combinations thereof. MHC-target models and MHC-off-target models can be generated computationally by de novo / ab initio approaches or by using one or more templates. For instance, such models can be generated computationally by fragment assembly (e.g., using Rosetta or other such tools), by template-based modeling / homology-based modeling / threading (e.g., using Rosetta or other such tools), by sequence-based machine learning (e.g., using AlphaFold or other such tools), or by other suitable computational tool as understood by a person skilled in the pertinent art, or combinations thereof. MHC-target models and MHC-off-target models can be generated using both experimental data and computational prediction tools. For instance, an initial 3D computational model or a portion of a 3D computational model may be determined by experimentation and the experimental-based 3D computational model (or model portion) may be refined or supplemented using computational tools.Attorney Docket #: 250298.000961 The terms “coarse-grained” and “refined”, when referring to a 3D computational model such as an MHC-target model and an MHC-off-target model, indicate a level of computational refinement performed on the 3D computational model to improve the accuracy and / or increase the resolution of the 3D computational model as compared to the physical structure that the 3D computational model represents. Generally, a “refined” 3D computational model is more accurate, higher resolution, and / or has been refined by more computational processing than a “coarse- grained” computational model. For instance, a coarse-grained model may be refined by minimizing some energy function or finding a minimum in an energy landscape (e.g., using Rosetta FlexPepDock, GROMOS force field, CHARMM force field, or other such tools). The term “connected” means that one function, feature, structure, or characteristic is directly joined to or in communication with another function, feature, structure, or characteristic. The term “coupled” means that one function, feature, structure, or characteristic is directly or indirectly joined to or in communication with another function, feature, structure, or characteristic. The terms “comprising” or “containing” or “including” are meant that at least the named element, or method step is present in article or method, but does not exclude the presence of other elements or method steps, even if the other such elements or method steps have the same function as what is named. As used herein, unless otherwise specified, the use of the ordinal adjectives “first,” “second,” “third,” etc., to describe a common object, merely indicate that different instances of like objects are being referred to, and are not intended to imply that the objects so described must be in a given sequence, either temporally, spatially, in ranking, or in any other manner. In this description, numerous specific details are set forth. It is to be understood, however, that implementations of the disclosed technology may be practiced without these specific details. In other instances, well-known methods, structures, and techniques have not been shown in detail in order not to obscure an understanding of this description. References to “one embodiment,” “an embodiment,” “some embodiments,” “example embodiment,” “various embodiments,” “one implementation,” “an implementation,” “example implementation,” “various implementations,” “some implementations,” etc., indicate that the implementation(s) of the disclosed technology so described may include a particular feature, structure, or characteristic, but not every implementation necessarily includes the particular feature, structure, or characteristic.Attorney Docket #: 250298.000961 Further, repeated use of the phrase “in one implementation” does not necessarily refer to the same implementation, although it may. DETAILED DESCRIPTION Embodiments presented herein provide in silico (i.e., computational) methods for 3D modeling of off-target peptides for comparison to target peptides. In certain aspects, methods presented herein can be used for the ultimate purpose of antigen-recognition molecule development. Being able to model and compare peptide conformations and peptide-in-groove structures in silico can provide valuable information so that laboratory and human testing can be more efficient and reduce adverse events in clinical trial testing. Embodiments presented herein generally relate to identification of off-target peptide(s) that are similar to an intended target peptide of an MHC-target peptide complex, such that an antigen-recognition molecule that is engineered for the intended target MHC-target peptide complex is likely to also target the off-target peptide(s). Embodiments presented herein provide methods for generating 3D models of off-targets and targets, comparing off-target models to target models, ranking off-targets for a given target based on structural similarity so that higher ranked off-targets may be used for further in vivo studies, and ranking potential targets based on similarity of potential off-targets so that higher ranked targets and their associated off-targets may be used for further in vivo studies. In some embodiments, ranking and identification of the off-targets and / or targets can be agnostic of the antigen-recognition molecule so that the identified off-target peptides, predicted in vivo toxicity, and / or ranking of potential target peptides can be used to guide development of an antigen-recognition molecule engineered to target a target peptide having a low number of identified off-target peptides, a low predicted probability of in vivo toxicity, and / or a preferred ranking. Some embodiments disclosed herein include computational systems, engines, modules, devices, and / or networks configured to carry out a majority of steps associated with the above embodiments. The output of such computational systems, etc. can be used to inform antigen-recognition molecule development, screening of patients for clinical trials, individual patient treatment, and other such applications as understood by a person skilled in the pertinent art according to the teachings herein. One aim of some embodiments presented herein is to avoid side effects that would otherwise be identified during clinical trials, thereby reducing patient death,Attorney Docket #: 250298.000961 reducing other adverse effects on patients, and reducing expenditure of time and resources in research and development. MHC molecules are generally classified into two categories: class I and class II MHC molecules. An MHC class I molecule is an integral membrane protein comprising a glycoprotein heavy chain, also referred to herein as the α chain, which has three extracellular domains (i.e., α1, α2 and α3) and two intracellular domains (i.e., a transmembrane domain (TM) and a cytoplasmic domain (CYT)). The heavy chain is noncovalently associated with a soluble subunit called β2 microglobulin (β2m or β2M). An MHC class II molecule or MHC class II protein is a heterodimeric integral membrane protein comprising one α chain and one β chain in noncovalent association. The α chain has two extracellular domains (α1 and α2), and two intracellular domains (a TM domain and a CYT domain). The β chain contains two extracellular domains (β1 and β2), and two intracellular domains (a TM domain and CYT domain). The domain organization of class I and class II MHC molecules forms the antigenic determinant binding site, e.g., the peptide-binding portion or peptide binding groove, of the MHC molecule. A peptide binding groove refers to a portion of an MHC protein that forms a cavity in which a peptide, e.g., antigenic determinant, can bind. The conformation of a peptide binding groove is capable of being altered upon binding of a peptide to enable proper alignment of amino acid residues important for TCR binding to the peptide-MHC (pMHC) complex. In some embodiments, MHC molecules include fragments of MHC chains that are sufficient to form a peptide binding groove. For example, a peptide binding groove of a class I protein can comprise portions of the α1 and α2 domains of the heavy chain capable of forming two β-pleated sheets and two α helices. Inclusion of a portion of the β2 microglobulin chain stabilizes the MHC class I molecule. While for most versions of MHC Class II molecules, interaction of the α and β chains can occur in the absence of a peptide, the two-chain molecule of MHC Class II is unstable until the binding groove is filled with a peptide. A peptide binding groove of a class II protein can comprise portions of the α1 and β1 domains capable of forming two β-pleated sheets and two α helices. A first portion of the α1 domain forms a first β-pleated sheet and a second portion of the α1 domain forms a first a helix. A first portion of the β1 domain forms a second β- pleated sheet and a second portion of the β1 domain forms a second a helix. The X-ray crystallographic structure of class II protein with a peptide engaged in the binding groove of the protein shows that one or both ends of the engaged peptide can project beyond the MHC proteinAttorney Docket #: 250298.000961 (Brown et al., pp. 33-39, 1993, Nature, Vol. 364; incorporated herein in its entirety by reference). Thus, the ends of the α1 and β1 α helices of class II form an open cavity such that the ends of the peptide bound to the binding groove are not buried in the cavity. Moreover, the X-ray crystallographic structure of class II proteins shows that the N-terminal end of the MHC β chain apparently projects from the side of the MHC protein in an unstructured manner since the first 4 amino acid residues of the β chain could not be assigned by X-ray crystallography. Many human and other mammalian MHCs are well known in the art. In some embodiments, the MHC molecule may be a human HLA molecule selected from the group consisting of HLA-A, HLA-B, HLA-C, HLA-E, HLA-F, and HLA-G. A list of commonly used HLA alleles is described in Shankarkumar et al. ((2004) The Human Leukocyte Antigen (HLA) System, Int. J. Hum. Genet. 4(2):91-103), incorporated herein in its entirety by reference. Shankarkumar et al. also present a brief explanation of HLA nomenclature used in the art. Additional information regarding HLA nomenclature and various HLA alleles can be found in Holdsworth et al. (2009) The HLA dictionary 2008: a summary of HLA-A, -B, -C, -DRB1 / 3 / 4 / 5, and DQB1 alleles and their association with serologically defined HLA-A, -B, -C, -DR, and -DQ antigens, Tissue Antigens 73:95-170, and a recent update by Marsh et al. (2010) Nomenclature for factors of the HLA system, 2010, Tissue Antigens 75:291-455, each of which publications is incorporated herein in its entirety by reference. In some embodiments, the MHC I or MHC II polypeptides may be derived from any functional human HLA-A, B, C, DR, or DQ molecules. In one embodiment, the HLA molecule is encoded by HLA-A2, such as an HLA-A*02:01 allele. In another embodiment, the HLA molecule is encoded by HLA-A1, such as an HLA-A*01:01 allele. Targeting peptide-MHC (pMHC) complexes specifically expressed on cells such as cancer cells via, e.g., antibody-based or cell-based therapeutics approaches, can be an effective way of destroying such cells. However, the potential off-targets associated with these pMHC complexes can often lead to off-target toxicity. The present disclosure provides, among other things, a method useful in the prediction of such off-targets. Methods useful in prediction of such off-targets are presented in WO2023122621A2, published June 29, 2023, which is incorporated by reference herein and attached as an Appendix hereto. In certain embodiments, WO2023122621A2 presents a method, referred to herein as the “PIGSPRED method” in which, for a target peptide, amino acid positions are distinguished as either being bound in an MHC-target peptide complex or available to bind to an antigenAttorney Docket #: 250298.000961 recognition molecule. In certain embodiments, the PIGSPRED method identifies potential off- target peptides based on binding affinity to the MHC molecule and the similarity of the amino acid sequence of a potential off-target peptide to the available positions of the target peptide. WO2023122621A2 at paragraphs

[0272] -

[0274] and Table 1B presents one example in which the PIGSPRED method is applied to a MAGEA4 target peptide GVYDGREHTV (SEQ ID NO: 242). In this example, positions 4 and 6-9 of said target peptide are identified as available positions, and potential off-target GLADGRTHTV (SEQ ID NO: 243) is determined a higher degree of similarity to said target peptide than other potential off-target peptides GVPDCRIFTV (SEQ ID NO: 244), SVYDAREFSV (SEQ ID NO: 245), GLSDGQWHTV (SEQ ID NO: 246), GVFDNCSHTV (SEQ ID NO: 247), and KVSDGHFHTV (SEQ ID NO: 248). In some embodiments, the PIGSPRED method calculates a DoS score, wherein only positions of the target peptide identified as not involved in interacting with the MHC molecule are considered in calculating the DoS score, and the PIGSPRED method calculates a probability of in vivo toxicity of each potential target peptide based at least in part on the DoS scores of the off- target peptide(s). Once cancer-specific pHLAs are identified, PIGSPRED can be used to calculate the number of potential off-targets having sequence similarity associated with each cancer-specific pHLA. In certain embodiments of the PIGSPRED method, the number of potential off-targets is representative of the likelihood of off-target toxicity associated with a target and is used to rank the list of pHLA targets and to prioritize the targets for therapeutic development. In certain embodiments of the PIGSPRED method, the off-targets predicted by PIGSPRED can be used in experimental screening of therapeutic molecules that do not bind the off-targets. The most specific therapeutic molecules can thus be selected for further development. Another method, referred to herein as “X-scan” determines antigen-recognition molecule (e.g., TCR) binding motifs. In some embodiments, the X-scan method can be used to determine positions of a target peptide which are important for binding to a respective antigen recognition molecule by: (i) generating a plurality of mutant peptides which have exactly one amino acid substitution at exactly one position of the target peptide; and (ii) determining which mutated peptides lead to increased or decreased signaling (e.g., TCR signaling) when brought into contact with the antigen-recognition molecule. Details of the X-scan method are described in greater detail in Border, Ellen C., et al. "Affinity-enhanced T-cell receptors for adoptive T-cell therapy targetingAttorney Docket #: 250298.000961 MAGE-A10: strategy for selection of an optimal candidate." Oncoimmunology 8.2 (2019), incorporated by reference herein in its entirety. In certain embodiments, the present disclosure provides computational methods based on 3D models of target and off-target peptides for ranking and / or selecting off-target peptides for use in in vitro methods for assessing off-target effects of an antigen-recognition molecule. In certain aspects, both the PIGSPRED method and the present disclosure describe methods which can be used to estimate off-target toxicity associated with a target peptide and identify potential off-target peptides for use in experimental screening of therapeutic molecules. In certain embodiments, systems and methods of the present disclosure can be utilized as an alternative to the PIGSPRED method; in certain embodiments, systems and methods of the present disclosure can incorporate or utilize the PIGSPRED method to pre-screen targets and / or off targets; in certain embodiments, systems and methods of the present disclosure can incorporate or utilize additional and / or alternative pre-screening methods to the PIGSPRED method; and in certain embodiments, a combination of similarity metrics determined by the PIGSPRED method (e.g., a probability of in vivo toxicity, risk metric, DoS, ranking) and / or alternative method can be used in combination with structural similarity metrics disclosed herein to prioritize target and / or off-target peptides for antigen-recognition molecule development. Various methods described herein may relate to identifying (e.g., ranking / selecting) target peptides and / or to identifying (e.g., ranking / selecting) off-target peptides for a given target peptide. Any of these methods may further comprise synthesizing a target peptide and / or one or more off-target peptides identified. Methods for peptide synthesis include those known in the art and described herein. Any of these methods may further comprise isolating (e.g., purifying) a target peptide and / or one or more off-target peptides identified. Methods for peptide isolation and / or purification include those known in the art and described herein. Any of these methods may further comprise loading a target peptide and / or one or more off-target peptides to an MHC molecule or any suitable component thereof to form a pMHC complex as described elsewhere herein. Any of these methods may further comprise binding a target peptide-MHC complex and / or one or more off-target peptide-MHC complexes to an antigen-recognition molecule (e.g., an antibody, TCR, or CAR). For example, any of these methods may comprise screening a target peptide-MHC complex and / or one or more off-target peptide MHC complexes for binding to an antigen-recognition molecule. Any of these methods may comprise incubating and / or contactingAttorney Docket #: 250298.000961 a target peptide and / or one or more off-target peptides with one or more cells (e.g., pulsing cells with peptide as described elsewhere herein). In a further aspect, provided herein are off-target peptides identified using the methods described herein. Accordingly, the present disclosure also provides libraries (e.g., target-specific libraries) comprising one or more of the off-target peptides identified using the methods described herein. In some embodiments, the libraries of the present disclosure may include the target peptides associated with the off-target peptides as well. In some embodiments, the libraries of the present disclosure may include off-target peptides identified by analyzing experimental structures of a pHLA in complex with an antigen-recognition molecule. In some embodiments, off-target peptides identified using the methods described herein may be identified for a Melanoma-Associated Antigen 3 (MAGE3) target peptide, e.g., for MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29). The MAGEA3 gene belongs to the MAGEA family, which comprises genes encoding proteins with significant sequence similarity, ranging from 50 to 80%. These genes are located at the Xq28 chromosomal region and exhibit variability in their promoters and first exons, allowing for diverse transcriptional regulation while maintaining functional consistency. MAGEA3 is a protein-coding gene linked to conditions such as, but not limited to, ocular melanoma and melanoma, and it plays a role in pathways like NF- kappaB signaling. MAGEA3 can function as an activator of ubiquitin ligase activity, influencing processes for example, without limitation, autophagy repression and tumor progression. Additionally, MAGEA3 is recognized by cytolytic T-lymphocytes in melanoma, highlighting its importance in cancer biology. In some embodiments, off-target peptides identified using the methods described herein may be identified for a Wilms Tumor 1 (WT1) target peptide, e.g., for WT1126-134 target RMFPNAPYL (SEQ ID NO: 241). The WT1 gene encodes a transcription factor characterized by four zinc-finger motifs at its C-terminus and a DNA-binding domain rich in proline and glutamine at the N-terminus. This gene can play a crucial role in the development of the urogenital system and can be associated with mutations in a subset of Wilms tumor patients. WT1 exhibits a complex pattern of tissue-specific imprinting, with varying expression from maternal and paternal alleles across different tissues. The WT1 gene has multiple transcript variants, some of which utilize a non-standard translation initiation codon. Additionally, WT1 mRNA can undergo tissue-specific RNA editing, which is developmentally regulated. Mutations in WT1 are linked to conditions suchAttorney Docket #: 250298.000961 as, but not limited to, acute myeloid leukemia, affecting prognosis and treatment resistance. The WT1 gene is involved in pathways related to sexual development and kidney function, and it has both tumor suppressor and oncogenic roles, depending on its isoform-specific functions. A variety of platforms for targeting MAGEA3 and / or WT1 are contemplated herein, such as, but not limited to, alternative format multispecific (e.g., bispecific) antibodies or antigen- binding fragments thereof, CAR T-cells (e.g., scFv-based CAR T cells) and engineered (T-cell receptor) TCR-T cells, and cancer vaccines. In one embodiment, anti-tumor TCRs may be engineered into T cells for cell-based therapy. In one embodiment, an anti-tumor TCR targeting MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29)-HLA-A*01:01 can be developed for an HLA-A*01:01 / MAGEA3168-176-targeted autologous TCR T cell therapy. In one embodiment, an anti-tumor TCR targeting WT1126-134target RMFPNAPYL (SEQ ID NO: 241)-HLA-A*02:01 can be developed for an HLA-A*02:01 / WT1126-134-targeted autologous TCR T cell therapy. Without wishing to be bound by theory, TCRs can be a promising therapeutic modality for the treatment of patients with solid tumors. TCRs greatly expand the repertoire of tumor antigens that can be targeted using immunotherapy, compared to CARs and traditional antibodies. Over 75% of proteins reside exclusively within intracellular compartments. Tumor-associated antigens (TAAs) and tumor-specific antigens (TSAs) typically consist of peptides derived from intracellular proteins that are loaded onto MHC. TCRs recognize tumor antigens via interactions with peptide-MHC (pMHC) complexes. Intracellular antigens undergo proteasomal cleavage to generate antigenic peptides. Peptides are transported into the ER, where they are further processed and loaded onto MHC. pMHC complexes are subsequently trafficked to the cell surface to enable extracellular presentation of intracellular antigens. TCRs are therefore a powerful tool that which can use to leverage the adaptive immune system in targeting and eliminating solid tumors. Ensuring tumor specificity of a target p-MHC is not enough for therapeutic TCR / antibody development; off-target toxicity remains a challenge. In some embodiments, the cancer is a hematologic malignancy, for example, a lymphoma, a leukemia, or a myeloma. In some embodiments, the lymphoma is Hodgkin's lymphoma or non-Hodgkin’s lymphoma. In some embodiments, the leukemia is chronic lymphocytic leukemia (CLL), acute lymphocytic leukemia (ALL), chronic myeloid leukemia (CML), or acute myeloid leukemia (AML). In some embodiments, the cancer is a solid cancer. InAttorney Docket #: 250298.000961 one embodiment, the cancer is a head and neck cancer. In one embodiment, the cancer is a renal cell carcinoma. In one embodiment, the cancer is a breast cancer, e.g., triple-negative breast cancer (TNBC). In one embodiment, the cancer is a non-small cell lung cancer (NSCLC), for example, lung adenocarcinoma. In one embodiment, the cancer is liver hepatocellular carcinoma (HCC). In one embodiment, the cancer is lung squamous cell carcinoma (SCC). In one embodiment, the cancer is bladder cancer. In one embodiment, the cancer is esophageal cancer. In one embodiment, the cancer is uveal melanoma. In one embodiment, the cancer is nasopharyngeal cancer. In one embodiment, the cancer is synovial sarcoma. In one embodiment, the cancer is ovarian cancer. In one embodiment, the cancer is uterine cancer. In one embodiment, the cancer is endometrial cancer. In one embodiment, the cancer is melanoma. In some embodiments, the cancer is selected from melanoma, non-small cell lung cancer (NSCLC), breast cancer, head and neck squamous cell carcinoma, bladder cancer, esophageal cancer, gastric cancer, ovarian cancer, and colorectal cancer. In some embodiments, the cancer is selected from Wilms tumor (i.e., nephroblastoma), acute myeloid leukemia, breast cancer, ovarian cancer, lung cancer, and prostate cancer. In various embodiments, a variety of platforms for targeting a MAGEA3 and / or WT1 are contemplated herein, such as, but not limited to, alternative format multispecific (e.g., bispecific) antibodies or antigen-binding fragments thereof, CAR T-cells (e.g., scFv-based CAR T cells) and engineered (T-cell receptor) TCR-T cells, and cancer vaccines. In one embodiment, anti-tumor TCRs may be engineered into T cells for cell-based therapy. In one embodiment, an anti-tumor TCR targeting MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29)-HLA-A*01:01 can be developed for an HLA-A*01:01 / MAGEA3168-176-targeted autologous TCR T cell therapy. In one embodiment, an anti-tumor TCR targeting WT1126-134 target RMFPNAPYL (SEQ ID NO: 241)- HLA-A*02:01 can be developed for an HLA-A*02:01 / WT1126-134-targeted autologous TCR T cell therapy. Without wishing to be bound by theory, TCRs can be a promising therapeutic modality for the treatment of patients with solid tumors. TCRs greatly expand the repertoire of tumor antigens that can be targeted using immunotherapy, compared to CARs and traditional antibodies. Over 75% of proteins reside exclusively within intracellular compartments. Tumor- associated antigens (TAAs) and tumor-specific antigens (TSAs) typically consist of peptides derived from intracellular proteins that are loaded onto MHC. TCRs recognize tumor antigens viaAttorney Docket #: 250298.000961 interactions with peptide-MHC (pMHC) complexes. Intracellular antigens undergo proteasomal cleavage to generate antigenic peptides. Peptides are transported into the ER, where they are further processed and loaded onto MHC. pMHC complexes are subsequently trafficked to the cell surface to enable extracellular presentation of intracellular antigens. TCRs are therefore a powerful tool that which can use to leverage the adaptive immune system in targeting and eliminating solid tumors. Ensuring tumor specificity of a target pMHC is not enough for therapeutic TCR / antibody development; off-target toxicity remains a challenge. In certain embodiments, the MAGEA3 and / or WT1 peptide described herein is wild type. In certain embodiments, the MAGEA3 and / or WT1 peptide described herein comprises a mutation (e.g., a deletion, a substitution, or an addition). Non-limiting examples of amino acid mutations comprise amino acid insertions, substitutions, and / or deletions. Inserted amino acid residues may be inserted at any position and inserted amino acid residues may be inserted in a way such that some of or all the inserted amino acid residues are immediately adjacent to one another or such that none of the inserted amino acid residues are immediately adjacent to one another. Amino acid substitution means exchanging an amino acid residue for a replacement amino acid residue at the same position. In some embodiments, the MAGEA3 peptide is a MAGEA3168-176 peptide having an amino acid sequence of EVDPIGHLY (SEQ ID NO: 29). See, e.g., NCBI Reference Sequences 5BRZ_C, NP_005353.1, BAD97239.1, KAI2601173.1, 4V0P_A, 8T9A_C, 9BD2_A, and KAI2601175.1, which are each herein incorporated by reference in their entirety. The peptide can be a peptide comprising about 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 18, 20, 25, 30, 35, 40, 50, 60, 70, 80, 90, or 100 amino acid residues of the MAGEA3 protein. In some embodiments, the WT1 peptide is a WT1126-134 peptide having an amino acid sequence of RMFPNAPYL (SEQ ID NO: 241). See, e.g., NCBI Reference Sequences KAI2559287.1 and 3HPJ_C, which are each herein incorporated by reference in their entirety. The peptide can be a peptide comprising about 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 18, 20, 25, 30, 35, 40, 50, 60, 70, 80, 90, or 100 amino acid residues of the MAGEA3 and / or WT1 protein. In some embodiments, the peptide comprises 9 amino acid residues. The substitution may be at any position along the length of the peptide. For example, it may be located in the C terminal third of the peptide, the central third of the peptide, or the N terminal third of the peptide.Attorney Docket #: 250298.000961 In some embodiments, the target peptide (e.g., MAGEA3168-176target peptide or WT1126-134target peptide) is 5-40 amino acids in length, or 5-33 amino acids in length, or 5-30 amino acids in length, or 5-23 amino acids in length, 5-20 amino acids in length, or 5-17 amino acids in length, or 5-14 amino acids in length, or 5-12 amino acids in length, or 5-11 amino acids in length, or 5- 10 amino acids in length, or 6-40 amino acids in length, or 6-33 amino acids in length, or 6-30 amino acids in length, or 6-23 amino acids in length, or 6-20 amino acids in length, or 6-17 amino acids in length, or 6-14 amino acids in length, or 6-12 amino acids in length, or 6-11 amino acids in length, or 6-10 amino acids in length, or 7-40 amino acids in length, or 7-33 amino acids in length, or 7-30 amino acids in length, or 7-23 amino acids in length, or 7-20 amino acids in length, or 7-17 amino acids in length, or 7-14 amino acids in length, or 7-12 amino acids in length, or 7- 11 amino acids in length, or 7-10 amino acids in length, or 8-40 amino acids in length, or 8-33 amino acids in length, or 8-30 amino acids in length, or 8-23 amino acids in length, or 8-20 amino acids in length, or 8-17 amino acids in length, or 8-14 amino acids in length, or 8-12 amino acids in length, or 8-11 amino acids in length, or 8-10 amino acids in length, or 9-40 amino acids in length, or 9-33 amino acids in length, 9-30 amino acids in length, or 9-23 amino acids in length, or 9-20 amino acids in length, or 9-17 amino acids in length, or 9-14 amino acids in length, or 9- 12 amino acids in length, or 9-11 amino acids in length, or 9-10 amino acids in length, or 10-40 amino acids in length, or 10-33 amino acids in length, or 10-30 amino acids in length, or 10-23 amino acids in length, or 10-20 amino acids in length, or 10-17 amino acids in length, or 10-14 amino acids in length, or 10-12 amino acids in length, or 10-11 amino acids in length, or 11-40 amino acids in length, or 11-33 amino acids in length, or 11-30 amino acids in length, or 11-23 amino acids in length, or 11-20 amino acids in length, or 11-17 amino acids in length, or 11-14 amino acids in length, or 11-12 amino acids in length, or 12-40 amino acids in length, or 12-33 amino acids in length, or 12-30 amino acids in length, or 12-23 amino acids in length, or 12-20 amino acids in length, or 12-17 amino acids in length, or 12-14 amino acids in length, or 40 amino acids in length, or 39 amino acids in length, or 38 amino acids in length, or 37 amino acids in length, or 36 amino acids in length, or 35 amino acids in length, or 34 amino acids in length, or 33 amino acids in length, or 32 amino acids in length, or 31 amino acids in length, or 30 amino acids in length, or 29 amino acids in length, or 28 amino acids in length, or 27 amino acids in length, or 26 amino acids in length, or 25 amino acids in length, or 24 amino acids in length, or 23 amino acids in length, or 22 amino acids in length, or 21 amino acids in length, or 20 amino acids inAttorney Docket #: 250298.000961 length, or 19 amino acids in length, or 18 amino acids in length, or 17 amino acids in length, or 16 amino acids in length, or 15 amino acids in length, or 14 amino acids in length, or 13 amino acids in length, or 12 amino acids in length, or 11 amino acids in length, or 10 amino acids in length, or 9 amino acids in length, or 8 amino acids in length, or 7 amino acids in length, or 6 amino acids in length, or 5 amino acids in length. In some embodiments, the target peptide (e.g., e.g., MAGEA3168-176 target peptide or WT1126-134 target peptide) is 5-30 amino acids in length, or 8-30 amino acids in length, or 8-20 amino acids in length, or 8-23 amino acids in length, or 8-17 amino acids in length, or 8-14 amino acids in length, or 8-12 amino acids in length, or 8-11 amino acids in length, or 8-10 amino acids in length, or 9-30 amino acids in length, or 9-20 amino acids in length, or 9-23 amino acids in length, or 9-17 amino acids in length, or 9-14 amino acids in length, or 9-12 amino acids in length, or 9-11 amino acids in length, or 9-10 amino acids in length, or 12-30 amino acids in length, or 12-23 amino acids in length, or 12-20 amino acids in length, or 12-17 amino acids in length, or 12-14 amino acids in length, or 12 amino acids in length, or 10 amino acids in length, or 9 amino acids in length. In various embodiments, a peptide library of the present disclosure may comprise one or more off-target peptides identified for MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) and / or WT1126-134target RMFPNAPYL (SEQ ID NO: 241) as described herein. In some embodiments, off-target peptides for MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) include those listed in Tables 2-4 herein (See Example 1). Tables 2-4 further include, e.g., the DoS (i.e., the degree of sequence similarity of the off-target peptide with the target peptide considering all amino acid positions); a ranked order as determined by a structural similarity metric (RMSD); the predicted binding affinity of each off-target peptide represented by the half maximal inhibitory concentration (IC50) value and a binding affinity percentile rank value; a description of the off- target gene corresponding to each of the off-target peptides; the mRNA level (TMP from GTEx) in the normal tissue with the highest expression for each off-target gene; as well as a description of which peptides were present in the internal immunopeptidomics database of MHC-bound peptides identified by mass spectrometry (Mass Spec) in tissue samples, as determined experimentally using exemplary methods of the disclosure. In some embodiments, off-target peptides for WT1126-134 target RMFPNAPYL (SEQ ID NO: 241) include those listed in Table 5 herein (See Example 2). Table 5 further includes, e.g., a description of the off-target geneAttorney Docket #: 250298.000961 corresponding to each of the off-target peptides; the DoS (i.e., the degree of sequence similarity of the off-target peptide with the target peptide considering all amino acid positions); a ranked order as determined by a structural similarity metric (RMSD); as well as ranking by important residue RMSD, as determined experimentally using exemplary methods of the disclosure In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) comprises an amino acid sequence of any of SEQ ID NOs: 30- 47 and 200-232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) consists essentially of an amino acid sequence of any of SEQ ID NOs: 30-47 and 200-232. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) consists of an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) comprises an amino acid sequence of any of SEQ ID NOs: 200- 232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) consists essentially of an amino acid sequence of any of SEQ ID NOs: 200-232. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) consists of an amino acid sequence of any one of SEQ ID NOs: 200-232. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) comprises an amino acid sequence of any of SEQ ID NOs: 200- 201, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) consists essentially of an amino acid sequence of any of SEQ ID NOs: 200-201. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) consists of an amino acid sequence of any one of SEQ ID NOs: 200-201. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) comprises an amino acid sequence of any of SEQ ID NOs: 202- 232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) consists essentially of an amino acid sequence of any of SEQ ID NOs: 202-232. In someAttorney Docket #: 250298.000961 embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) consists of an amino acid sequence of any one of SEQ ID NOs: 202-232. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) comprises an amino acid sequence of any of SEQ ID NOs: 202- 230, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) consists essentially of an amino acid sequence of any of SEQ ID NOs: 202-230. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) consists of an amino acid sequence of any one of SEQ ID NOs: 202-230. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) comprises an amino acid sequence of any of SEQ ID NOs: 209, 231, and 232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) consists essentially of an amino acid sequence of any of SEQ ID NOs: 209, 231, and 232. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) consists of an amino acid sequence of any one of SEQ ID NOs: 209, 231, and 232. In some embodiments, an off-target peptide associated with WT1126-134target RMFPNAPYL (SEQ ID NO: 241) comprises an amino acid sequence of any of SEQ ID NOs 233- 240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with WT1126-134target RMFPNAPYL (SEQ ID NO: 241) consists essentially of an amino acid sequence of any of SEQ ID NOs: 233-240. In some embodiments, an off-target peptide associated with WT1126-134 target RMFPNAPYL (SEQ ID NO: 241) consists of an amino acid sequence of any one of SEQ ID NOs: 233-240. In various embodiments, a peptide library of one or more off-target peptides for an identified target peptide may further comprise the target peptide itself (e.g., MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) or WT1126-134target RMFPNAPYL (SEQ ID NO: 241)). In some embodiments, the target peptide comprises an amino acid sequence of SEQ ID NO: 29 or 241, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, the target peptide consists essentially of an amino acid sequence of SEQ ID NO: 29 or 241. In some embodiments, the target peptide consists of an amino acid sequence of SEQ IDAttorney Docket #: 250298.000961 NO: 29 or 241. In various embodiments, a peptide library of one or more off-target peptides for an identified target peptide, optionally including the target peptide itself (e.g., MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) and / or WT1126-134 target RMFPNAPYL (SEQ ID NO: 241)) may further include other variants of the target peptide, such as a wild-type / non-mutated version of the target peptide. The target peptide and / or wild-type version of the target peptide may be used, for example, in comparison studies with the one or more off-target peptides, such as to assess antigen-recognition molecule cross-reactivity with off-target peptides. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) may be cross-reactive to an antigen-recognition molecule targeting MAGEA3168-176 such as an antibody or TCR, e.g., a MAGEA3 TCR. In some embodiments, an antigen-recognition molecule described herein, such as an antibody or TCR, may react to cells that present MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) in complex with HLA-A*01:01 on a cell surface. In some embodiments, an antigen-recognition molecule, such as an antibody or TCR, may be cross-reactive with an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29). In some embodiments, an off-target peptide associated with WT1126-134 target RMFPNAPYL (SEQ ID NO: 241) may be cross-reactive to an antigen-recognition molecule targeting WT1126-134such as an antibody or TCR, e.g., a WT1 TCR. In some embodiments, an antigen-recognition molecule, such as an antibody or TCR, may react to cells that present WT1126- 134 target RMFPNAPYL (SEQ ID NO: 241) in complex with HLA-A*02:01 on a cell surface. In some embodiments, an antigen-recognition molecule, such as an antibody or TCR, may be cross- reactive with an off-target peptide associated with WT1126-134target RMFPNAPYL (SEQ ID NO: 241). In specific embodiments, the antigen-recognition molecule (e.g., WT1 TCR) is cross- reactive with ILF2127-135off-target KILPTLEAV (SEQ ID NO: 233) (ILF2 (Interleukin Enhancer Binding Factor 2) gene); RBM4B59-67off-target KLHGVNIN (SEQ ID NO: 234) (RBM4B (RNA Binding Motif Protein 4B) gene); SF3B478-86 off-target KLYGKPIRV (SEQ ID NO: 235) (SF3B4 (Splicing Factor 3b Subunit 4) gene); SHC1469-477off-target RVPPPPQSV (SEQ ID NO: 236) (SHC (Src Homology 2 Domain-Containing) Transforming Protein 1) gene); ARHGEF26863-871off-target RLLGLETNV (SEQ ID NO: 237) (ARHGEF26 (Rho Guanine Nucleotide Exchange Factor 26) gene); CRYL1130-138 off-target KLFAGLVHV (SEQ ID NO: 238) (CRYL1 (Crystallin Lambda 1) gene); CYP2C859-67off-target KVYGPVFTV (SEQ ID NO: 239) (CYP2C8Attorney Docket #: 250298.000961 (Cytochrome P450 Family 2 Subfamily C Member 8) gene); and / or USP9Y1674-1682off-target (USP9Y (Ubiquitin Specific Peptidase 9 Y-Linked) gene). In some embodiments, the off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) and / or WT1126-134target RMFPNAPYL (SEQ ID NO: 241) has 9 amino acids. In some embodiments, the off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) and / or WT1126-134 target RMFPNAPYL (SEQ ID NO: 241) can have a similar conformation to MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) and / or WT1126-134target RMFPNAPYL (SEQ ID NO: 241), for example, at TCR interacting residue positions determined to be important for TCR interaction (e.g., backbone residues at positions 4, 5, 6, and 8). In some embodiments, off-target peptides of a MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29)-HLA-A*01:01 complex can be ranked according to root mean square deviation (RMSD) of the respective off-target peptide backbone conformation relative to the target peptide backbone conformation. The off-target peptides can be sorted by median RMSD value, e.g., for the 5, 10, 15, 20, 25, 30, 40, 50, or 100 refined lowest energy MHC-off-target models. A lower RMSD value can indicate a higher degree of structural similarity. Non-limiting examples of off- target peptides having a high degree of structural similarity relative to the target peptide include off-target peptides having the amino acid sequence of SEQ ID NOs: 30-47 and 200-232. In some embodiments, an off-target peptide may be non-reactive to a TCR (e.g., a MAGEA3 TCR) as determined by exemplary method described herein. Such off-target peptide may have a dissimilar conformation to the MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29). In some embodiments, off-target peptides of a WT1126-134target RMFPNAPYL (SEQ ID NO: 241)-HLA-A*02:01 complex can be ranked according to root mean square deviation (RMSD) of the respective off-target peptide backbone conformation relative to the target peptide backbone conformation. The off-target peptides can be sorted by median RMSD value, e.g., for the 5, 10, 15, 20, 25, 30.40, 50, or 100 refined lowest energy MHC-off-target models. A lower RMSD value can indicate a higher degree of structural similarity. Non-limiting examples of off-target peptides having a high degree of structural similarity relative to the target peptide include off-target peptides having the amino acid sequence of SEQ ID NOs: 233-240. In some embodiments, an off-target peptide may be non-reactive to a TCR (e.g., a WT1 TCR) as determined by exemplary methodAttorney Docket #: 250298.000961 described herein. Such off-target peptide may have a dissimilar conformation to the WT1126-134target RMFPNAPYL (SEQ ID NO: 241). In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) comprises an amino acid sequence of any of SEQ ID NOs: 30- 47 and 200-232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) consists essentially of an amino acid sequence of any of SEQ ID NOs: 30-47 and 200-232. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) consists of an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) comprises an amino acid sequence of any of SEQ ID NOs: 200- 232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) consists essentially of an amino acid sequence of any of SEQ ID NOs: 200-232. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) consists of an amino acid sequence of any one of SEQ ID NOs: 200-232. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) comprises an amino acid sequence of any of SEQ ID NOs: 200- 201, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) consists essentially of an amino acid sequence of any of SEQ ID NOs: 200-201. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) consists of an amino acid sequence of any one of SEQ ID NOs: 200-201. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) comprises an amino acid sequence of any of SEQ ID NOs: 202- 232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) consists essentially of an amino acid sequence of any of SEQ ID NOs: 202-232. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) consists of an amino acid sequence of any one of SEQ ID NOs: 202-232.Attorney Docket #: 250298.000961 In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) comprises an amino acid sequence of any of SEQ ID NOs: 202- 230, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) consists essentially of an amino acid sequence of any of SEQ ID NOs: 202-230. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) consists of an amino acid sequence of any one of SEQ ID NOs: 202-230. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) comprises an amino acid sequence of any of SEQ ID NOs: 209, 231, and 232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) consists essentially of an amino acid sequence of any of SEQ ID NOs: 209, 231, and 232. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) consists of an amino acid sequence of any one of SEQ ID NOs: 209, 231, and 232. In some embodiments, an off-target peptide associated with WT1126-134 target RMFPNAPYL (SEQ ID NO: 241) comprises an amino acid sequence of any of SEQ ID NOs: 233- 240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with WT1126-134 target RMFPNAPYL (SEQ ID NO: 241) consists essentially of an amino acid sequence of any of SEQ ID NOs: 233-240. In some embodiments, an off-target peptide associated with WT1126-134target RMFPNAPYL (SEQ ID NO: 241) consists of an amino acid sequence of any one of SEQ ID NOs: 233-240. In some embodiments, a peptide library comprising off-target peptides described herein may comprise two or more of any of various off-target peptides described herein. As a non-limiting example, a peptide library comprising off-target peptides may comprise two or more peptides each selected from the amino acid sequences of SEQ ID NOs: 30-47 and 200-232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative. As another non-limiting example, a peptide library comprising off-target peptides may comprise two or more peptides each selected from the amino acid sequences of SEQ ID NOs: 200-232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative. As yet another non-limiting example, a peptide library comprising off- target peptides may comprise two or more peptides each selected from the amino acid sequencesAttorney Docket #: 250298.000961 of SEQ ID NOs: 200-201, or a pharmaceutically acceptable salt thereof, or a fragment or derivative. In some embodiments, a peptide library comprising off-target peptides may comprise two or more peptides each selected from the amino acid sequences of SEQ ID NOs: 202-232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative. In some embodiments, a peptide library comprising off-target peptides may comprise two or more peptides each selected from the amino acid sequences of SEQ ID NOs: 202-230, or a pharmaceutically acceptable salt thereof, or a fragment or derivative. In some embodiments, a peptide library comprising off-target peptides may comprise two or more peptides each selected from the amino acid sequences of SEQ ID NOs: 209, 231, and 232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative. In some embodiments, a peptide library comprising off-target peptides may comprise two or more peptides each selected from the amino acid sequences of SEQ ID NOs: 233-240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative. In a specific embodiment, the isolated peptide can be, e.g., 8-12 amino acids in length. In a specific embodiment, the isolated peptide can be 9-12 amino acids in length. In a specific embodiment, the off-target peptide, or fragment or derivative thereof, can be, e.g., 8-14 amino acids in length, for example 9 amino acids in length. In another specific embodiment, the off-target peptide, or fragment or derivative thereof, can be, e.g., 12-20 amino acids in length. In some embodiments, the peptides within a peptide library described herein can each present in a complex with a major histocompatibility complex (MHC) molecule described herein. In certain embodiments, the MHC molecule is a class I MHC molecule such as, but not limited to, a class I human leukocyte antigen (HLA) molecule. The class I human leukocyte antigen (HLA) molecule can be an HLA-A molecule. In some embodiments, the HLA-A molecule is an HLA-A2 molecule. In some specific embodiments, the HLA-A2 molecule is an HLA-A*02:01 molecule. In some embodiments, the HLA-A molecule is an HLA-A1 molecule. In some specific embodiments, the HLA-A1 molecule is an HLA-A*01:01molecule. In some embodiments, a peptide within an MHC-peptide complex described herein, e.g., a MAGEA3168-176peptide complex, and / or an MHC-off-target peptide complex described herein, e.g., an MHC-off-target peptide complex comprising an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29), can be covalently bound to an MHC described herein.Attorney Docket #: 250298.000961 In some embodiments, a peptide within an MHC-peptide complex described herein, e.g., a MAGEA3168-176peptide complex , and / or an MHC-off-target peptide complex described herein, e.g., an MHC-off-target peptide complex comprising an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29), can be non-covalently bound to an MHC described herein. In some embodiments, a peptide within an MHC-peptide complex described herein, e.g., a WT1126-134 peptide complex, and / or an MHC-off-target peptide complex described herein, e.g., an MHC-off-target peptide complex comprising an off-target peptide associated with WT1126-134target RMFPNAPYL (SEQ ID NO: 241), can be covalently bound to an MHC described herein. In some embodiments, a peptide within an MHC-peptide complex described herein, e.g., a WT1126-134peptide complex , and / or an MHC-off-target peptide complex described herein, e.g., an MHC-off-target peptide complex comprising an off-target peptide associated with WT1126-134target RMFPNAPYL (SEQ ID NO: 241), can be non-covalently bound to an MHC described herein. In various embodiments, the present disclosure provides a library comprising two or more proteins or fragments thereof each comprising one or more off-target peptides described herein. In some embodiments, each off-target peptide can be selected from the amino acid sequences of SEQ ID NOs: 30-47 and 200-232. In some embodiments, each off-target peptide can be selected from the amino acid sequences of SEQ ID NOs: 200-232. In some embodiments, each off-target peptide can be selected from the amino acid sequences of SEQ ID NOs: 200-201. In some embodiments, each off-target peptide can be selected from the amino acid sequences of SEQ ID NOs: 202-232. In some embodiments, each off-target peptide can be selected from the amino acid sequences of SEQ ID NOs: 202-230. In some embodiments, each off-target peptide can be selected from the amino acid sequences of SEQ ID NOs: 209, 231, and 232. In some embodiments, each off-target peptide can be selected from the amino acid sequences of SEQ ID NOs: 233-240. Peptide libraries of present disclosure may comprise any number of a plurality of peptides as desired. For example, a peptide library of the present disclosure may comprise at least 2 peptides, at least 3 peptides, at least 4 peptides, at least 5 peptides, at least 6 peptides, at least 7 peptides, at least 8 peptides, at least 9 peptides, at least 10 peptides, at least 20 peptides, at least 30 peptides, at least 40 peptides, at least 50 peptides, or about 2-5 peptides, about 2-10 peptides, about 5-15 peptides, about 10-20 peptides, about 10-30 peptides, about 12-25 peptides, about 20-Attorney Docket #: 250298.000961 30 peptides, about 25-50 peptides, about 40-80 peptides, about 50-100 peptides, about 60-120 peptides, about 70-140 peptides, about 80-160 peptides, about 90-180 peptides, about 100-200 peptides, about 110-220 peptides, about 120-240 peptides, about 130-260 peptides, about 140-280 peptides, about 150-300 peptides, about 160-320 peptides, about 170-340 peptides, about 180-360 peptides, about 190-380 peptides, about 200-400 peptides, about 210-420 peptides, about 220-440 peptides, about 230-460 peptides, about 240-480 peptides, about 250-500 peptides, about 260-520 peptides, about 270-540 peptides, about 280-560 peptides, about 290-580 peptides, about 300-600 peptides, about 310-620 peptides, about 320-640 peptides, about 330-660 peptides, about 340-680 peptides, about 350-700 peptides, about 360-720 peptides, about 370-740 peptides, about 380-760 peptides, about 390-780 peptides, about 400-800 peptides, about 410-820 peptides, about 420-840 peptides, about 430-860 peptides, about 440-880 peptides, about 450-900 peptides, about 460-920 peptides, about 470-940 peptides, about 480-960 peptides, about 490-980 peptides, about 500- 1000 peptides, etc. In a further aspect, provided herein are databases including computational representations of the off-target peptides identified using the methods described herein. The database can include information for each of the off-target peptides represented in any one of the exemplary libraries disclosed hereinabove. Accordingly, the databases may include computational representations of the target peptides associated with the off-target peptides as well. The computer-readable representations of the peptides in the database can include a peptide sequence or a computer model of the peptide. A peptide of the disclosure may be synthetically produced or produced by hydrolysis. Synthetically produced peptides can include randomly generated peptides, specifically designed peptides, and peptides where at least some of the amino acid positions are conserved among several peptides and the remaining positions are random. Alternatively, a peptide of the present disclosure may be produced by expression in a heterologous host cell. In some embodiments, peptides of the disclosure can be synthesized by e.g., solid phase synthesis. As such, the peptides may be immobilized, for example to a solid support such as a bead. Peptides of the disclosure may be synthesized by the Fmoc-polyamide mode of solid-phase peptide synthesis. Temporary N-amino group protection is afforded by the 9- fluorenylmethyloxycarbonyl (Fmoc) group. Repetitive cleavage of this highly base-labile protecting group is done using 20% piperidine in N, N-dimethylformamide. Side-chainAttorney Docket #: 250298.000961 functionalities may be protected as their butyl ethers (in the case of serine threonine and tyrosine), butyl esters (in the case of glutamic acid and aspartic acid), butyloxycarbonyl derivative (in the case of lysine and histidine), trityl derivative (in the case of cysteine) and 4-methoxy-2,3,6- trimethylbenzenesulphonyl derivative (in the case of arginine). Where glutamine or asparagine are C-terminal residues, use is made of the 4,4′-dimethoxybenzhydryl group for protection of the side chain amido functionalities. The solid-phase support is based on a polydimethyl-acrylamide polymer constituted from the three monomers dimethylacrylamide (backbone-monomer), bisacryloylethylene diamine (cross linker) and acryloylsarcosine methyl ester (functionalizing agent). The peptide-to-resin cleavable linked agent used is the acid-labile 4-hydroxymethyl- phenoxyacetic acid derivative. All amino acid derivatives are added as their preformed symmetrical anhydride derivatives except for asparagine and glutamine, which are added using a reversed N, N-dicyclohexyl-carbodiimide / 1-hydroxybenzotriazole mediated coupling procedure. All coupling and deprotection reactions are monitored using ninhydrin, trinitrobenzene sulphonic acid or isotin test procedures. Upon completion of synthesis, peptides are cleaved from the resin support with concomitant removal of side-chain protecting groups by treatment with 95% trifluoroacetic acid containing a 50% scavenger mix. Scavengers commonly used include ethanedithiol, phenol, anisole and water, the exact choice depending on the constituent amino acids of the peptide being synthesized. Also, a combination of solid phase and solution phase methodologies for the synthesis of peptides is possible. Trifluoroacetic acid is removed by evaporation in vacuo, with subsequent trituration with diethyl ether affording the crude peptide. Any scavengers present are removed by a simple extraction procedure which on lyophilization of the aqueous phase affords the crude peptide free of scavengers. Purification may be performed by techniques such as re-crystallization, ion-exchange chromatography, size exclusion chromatography, hydrophobic interaction chromatography and reverse-phase high performance liquid chromatography using e.g., acetonitrile / water gradient separation, or a combination thereof. Peptides may be analyzed using thin layer chromatography, electrophoresis, in particular capillary electrophoresis, solid phase extraction (CSPE), reverse-phase high performance liquid chromatography, amino-acid analysis after acid hydrolysis and by fast atom bombardment (FAB) mass spectrometric analysis, as well as MALDI and ESI-Q-TOF mass spectrometric analysis.Attorney Docket #: 250298.000961 Alternatively, the peptide may be produced by recombinant expression in a heterologous host cell. Such methods typically involve the use of a vector comprising a nucleic acid sequence encoding the peptide to be expressed, to express the polypeptide in vivo; for example, in bacteria, yeast, insect or mammalian cells. In further embodiments, in vitro cell-free systems may be used. The peptides may be isolated and / or may be provided in substantially pure form. For example, they may be provided in a form which is substantially free of other peptides or proteins. A peptide, or fragment or derivative thereof, disclosed herein (e.g., an isolated peptide, an off-target peptide, a target peptide, a peptide within a peptide library, a peptide within an MHC- peptide complex, etc.) may vary in length. In some embodiments, the peptides of the disclosure may be 5-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-9 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-10 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-11 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-12 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-13 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-14 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-15 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-16 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-17 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-18 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-19 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-20 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-23 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-28 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 5-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-40 amino acids in length. In various embodiments, the peptides of the disclosure may be 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, or 40 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-9 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-10 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-11 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-12 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-13 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-14 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-15 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-16 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-17 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-18 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-19 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-20 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-23 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 6-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 6-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-9 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-10 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-11 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-12 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-13 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-14 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-15 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-16 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-17 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-18 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-19 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-20 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-21 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 7-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-23 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 7-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-9 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-10 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-11 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-12 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-13 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-14 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-15 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-16 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-17 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-18 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-19 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 8-20 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-23 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 8-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-10 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-11 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-12 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-13 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-14 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-15 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-16 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-17 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-18 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 9-19 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-20 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-23 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 9-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-11 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-12 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-13 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-14 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-15 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-16 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-17 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-18 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 10-19 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-20 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-23 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 10-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-12 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-13 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-14 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-15 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-16 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-17 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-18 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-19 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 11-20 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-23 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-25 amino in length. In someembodiments, the peptides of the disclosure may be 11-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-27 amino in length. In someembodiments, the peptides of the disclosure may be 11-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-29 amino in length. In someembodiments, the peptides of the disclosure may be 11-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-35 aminoin length. In some embodiments, the peptides of the disclosure may be 11-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-37 aminoin length. In some embodiments, the peptides of the disclosure may be 11-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 11-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-16 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-13 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-14 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-15 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-16 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-17 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-18 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-19 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-20 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 12-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-23 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-26 amino in length. In someembodiments, the peptides of the disclosure may be 12-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-28 amino in length. In someembodiments, the peptides of the disclosure may be 12-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-30 amino in length. In someembodiments, the peptides of the disclosure may be 12-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-36 aminoin length. In some embodiments, the peptides of the disclosure may be 12-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-38 aminoin length. In some embodiments, the peptides of the disclosure may be 12-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 12-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-14 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-15 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-16 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-17 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-18 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-19 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-20 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-23 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 13-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-29 amino in length. In someembodiments, the peptides of the disclosure may be 13-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-31 amino in length. In someembodiments, the peptides of the disclosure may be 13-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-33 amino in length. In someembodiments, the peptides of the disclosure may be 13-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 13-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-15 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-16 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-17 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-18 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-19 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-20 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-23 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-28 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 14-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 14-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-16 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-17 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-18 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-19 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-20 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-23 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-34 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 15-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 15-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-17 amino acids in length. In some In some embodiments, the peptides of the disclosure may be 16-18 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-19 amino acids in length. embodiments, the peptides of the disclosure may be 16-20 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-23 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 16-40 amino acids in length.Attorney Docket #: 250298.000961 In some embodiments, the peptides of the disclosure may be 17-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 17-18 amino acids in length. In some embodiments, the peptides of the disclosure may be 17-19 amino acids in length. In some embodiments, the peptides of the disclosure may be 17-20 amino acids in length. In some embodiments, the peptides of the disclosure may be 17-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 17-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 17-23 amino in length. In someembodiments, the peptides of the disclosure may be 17-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 17-25 amino in length. In someembodiments, the peptides of the disclosure may be 17-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 17-27 aminoin length. In some embodiments, the peptides of the disclosure may be 17-28 aminoin length. In some embodiments, the peptides of the disclosure may be 17-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 17-30 aminoin length. In some embodiments, the peptides of the disclosure may be 17-31 aminoin length. In some embodiments, the peptides of the disclosure may be 17-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 17-33 aminoin length. In some embodiments, the peptides of the disclosure may be 17-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 17-35 aminoin length. In some embodiments, the peptides of the disclosure may be 17-36 aminoin length. In some embodiments, the peptides of the disclosure may be 17-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 17-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 17-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 17-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-19 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-20 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-23 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 18-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-29 amino in length. In someembodiments, the peptides of the disclosure may be 18-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-31 amino in length. In someembodiments, the peptides of the disclosure may be 18-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-33 amino in length. In someembodiments, the peptides of the disclosure may be 18-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 18-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-20 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-23 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-32 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 19-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 19-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-21 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-23 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-25 aminoin length. In some embodiments, the peptides of the disclosure may be 20-26 aminoin length. In some embodiments, the peptides of the disclosure may be 20-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-28 aminoin length. In some embodiments, the peptides of the disclosure may be 20-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-30 aminoin length. In some embodiments, the peptides of the disclosure may be 20-31 aminoin length. In some embodiments, the peptides of the disclosure may be 20-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 20-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-22 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 21-22 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-28 amino in length. In someembodiments, the peptides of the disclosure may be 21-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-30 amino in length. In someembodiments, the peptides of the disclosure may be 21-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-32 amino in length. In someembodiments, the peptides of the disclosure may be 21-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 21-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-23 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-34 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 22-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 22-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-24 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-27 amino acids in length. In some embodiments, peptides of the disclosure may be 23-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 23-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-25 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-30 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 24-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 24-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-26 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 25-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 26-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 26-27 amino acids in length. In some embodiments, the peptides of the disclosure may be 26-28 amino acids in length. In some embodiments, the peptides of the disclosure may be 26-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 26-30 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 26-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 26-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 26-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 26-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 26-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 26-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 26-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 26-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 26-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 26-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 27-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 27-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 27-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 27-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 27-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 27-35 aminoin length. In some embodiments, the peptides of the disclosure may be 27-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 27-37 aminoin length. In some embodiments, the peptides of the disclosure may be 27-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 27-39 aminoin length. In some embodiments, the peptides of the disclosure may be 27-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 28-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 28-29 amino acids in length. In some embodiments, the peptides of the disclosure may be 28-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 28-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 28-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 28-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 28-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 28-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 28-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 28-37 amino acids in length. In someAttorney Docket #: 250298.000961 embodiments, the peptides of the disclosure may be 28-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 28-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 28-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 29-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 29-30 amino acids in length. In some embodiments, the peptides of the disclosure may be 29-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 29-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 29-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 29-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 29-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 29-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 29-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 29-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 29-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 29-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 30-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 30-31 amino acids in length. In some embodiments, the peptides of the disclosure may be 30-32 amino acids in length. In some embodiments, the peptides of the disclosure may be 30-33 amino acids in length. In some embodiments, the peptides of the disclosure may be 30-34 amino acids in length. In some embodiments, the peptides of the disclosure may be 30-35 amino acids in length. In some embodiments, the peptides of the disclosure may be 30-36 amino acids in length. In some embodiments, the peptides of the disclosure may be 30-37 amino acids in length. In some embodiments, the peptides of the disclosure may be 30-38 amino acids in length. In some embodiments, the peptides of the disclosure may be 30-39 amino acids in length. In some embodiments, the peptides of the disclosure may be 30-40 amino acids in length. In some embodiments, the peptides of the disclosure may be 5-40 amino acids in length, or 5-33 amino acids in length, or 5-30 amino acids in length, or 5-23 amino acids in length, 5-20 amino acids in length, or 5-17 amino acids in length, or 5-14 amino acids in length, or 5-12 amino acids in length, or 5-11 amino acids in length, or 5-10 amino acids in length, or 6-40 amino acids in length, or 6-33 amino acids in length, or 6-30 amino acids in length, or 6-23 amino acids inAttorney Docket #: 250298.000961 length, or 6-20 amino acids in length, or 6-17 amino acids in length, or 6-14 amino acids in length, or 6-12 amino acids in length, or 6-11 amino acids in length, or 6-10 amino acids in length, or 7- 40 amino acids in length, or 7-33 amino acids in length, or 7-30 amino acids in length, or 7-23 amino acids in length, or 7-20 amino acids in length, or 7-17 amino acids in length, or 7-14 amino acids in length, or 7-12 amino acids in length, or 7-11 amino acids in length, or 7-10 amino acids in length, or 8-40 amino acids in length, or 8-33 amino acids in length, or 8-30 amino acids in length, or 8-23 amino acids in length, or 8-20 amino acids in length, or 8-17 amino acids in length, or 8-14 amino acids in length, or 8-12 amino acids in length, or 8-11 amino acids in length, or 8- 10 amino acids in length, or 9-40 amino acids in length, or 9-33 amino acids in length, 9-30 amino acids in length, or 9-23 amino acids in length, or 9-20 amino acids in length, or 9-17 amino acids in length, or 9-14 amino acids in length, or 9-12 amino acids in length, or 9-11 amino acids in length, or 9-10 amino acids in length, or 10-40 amino acids in length, or 10-33 amino acids in length, or 10-30 amino acids in length, or 10-23 amino acids in length, or 10-20 amino acids in length, or 10-17 amino acids in length, or 10-14 amino acids in length, or 10-12 amino acids in length, or 10-11 amino acids in length, or 11-40 amino acids in length, or 11-33 amino acids in length, or 11-30 amino acids in length, or 11-23 amino acids in length, or 11-20 amino acids in length, or 11-17 amino acids in length, or 11-14 amino acids in length, or 11-12 amino acids in length, or 12-40 amino acids in length, or 12-33 amino acids in length, or 12-30 amino acids in length, or 12-23 amino acids in length, or 12-20 amino acids in length, or 12-17 amino acids in length, or 12-14 amino acids in length, or 40 amino acids in length, or 39 amino acids in length, or 38 amino acids in length, or 37 amino acids in length, or 36 amino acids in length, or 35 amino acids in length, or 34 amino acids in length, or 33 amino acids in length, or 32 amino acids in length, or 31 amino acids in length, or 30 amino acids in length, or 29 amino acids in length, or 28 amino acids in length, or 27 amino acids in length, or 26 amino acids in length, or 25 amino acids in length, or 24 amino acids in length, or 23 amino acids in length, or 22 amino acids in length, or 21 amino acids in length, or 20 amino acids in length, or 19 amino acids in length, or 18 amino acids in length, or 17 amino acids in length, or 16 amino acids in length, or 15 amino acids in length, or 14 amino acids in length, or 13 amino acids in length, or 12 amino acids in length, or 11 amino acids in length, or 10 amino acids in length, or 9 amino acids in length, or 8 amino acids in length, or 7 amino acids in length, or 6 amino acids in length, or 5 amino acids in length.Attorney Docket #: 250298.000961 In some embodiments, the peptides of the disclosure may be 5-30 amino acids in length, or 8-30 amino acids in length, or 8-20 amino acids in length, or 8-23 amino acids in length, or 8- 17 amino acids in length, or 8-14 amino acids in length, or 8-12 amino acids in length, or 8-11 amino acids in length, or 8-10 amino acids in length, or 9-30 amino acids in length, or 9-20 amino acids in length, or 9-23 amino acids in length, or 9-17 amino acids in length, or 9-14 amino acids in length, or 9-12 amino acids in length, or 9-11 amino acids in length, or 9-10 amino acids in length, or 12-30 amino acids in length, or 12-23 amino acids in length, or 12-20 amino acids in length, or 12-17 amino acids in length, or 12-14 amino acids in length, or 12 amino acids in length, or 10 amino acids in length, or 9 amino acids in length. The peptides of the disclosure may comprise one or more chemical modifications. Non- limiting examples of chemical modifications include, for example, phosphorylation, acetylation, deamidation acylation, amidination, pyridoxylation of lysine, reductive alkylation, trinitrobenzylation of amino groups with 2,4,6-trinitrobenzene sulphonic acid (TNBS), amide modification of carboxyl groups and sulphydryl modification by performic acid oxidation of cysteine to cysteic acid, formation of mercurial derivatives, formation of mixed disulfides with other thiol compounds, reaction with maleimide, carboxymethylation with iodoacetic acid or iodoacetamide and carbamoylation with cyanate at alkaline pH. Chemical modifications may correspond to those that are not present in vivo. For example, modification of, for example, arginyl residues in proteins may be based on the reaction of vicinal dicarbonyl compounds such as phenylglyoxal, 2,3-butanedione, and 1,2- cyclohexanedione to form an adduct. Another example is the reaction of methylglyoxal with arginine residues. Cysteine can be modified without concomitant modification of other nucleophilic sites such as lysine and histidine. Selective reduction of disulfide bonds in proteins can also be performed. Disulfide bonds can be formed and oxidized during the heat treatment of biopharmaceuticals. Woodward’s Reagent K may be used to modify specific glutamic acid residues. N-(3-(dimethylamino)propyl)-N′-ethylcarbodiimide can be used to form intra-molecular crosslinks between a lysine residue and a glutamic acid residue. For example, diethylpyrocarbonate and 4-hydroxy-2-nonenal can be used to modify histidyl residues in proteins. The reaction of lysine residues and other α-amino groups is, for example, useful in binding of peptides to surfaces or the cross-linking of proteins / peptides. Lysine is the site of attachment of poly(ethylene)glycol and the major site of modification in the glycosylation of proteins.Attorney Docket #: 250298.000961 Methionine residues in proteins can be modified with e.g., iodoacetamide, bromoethylamine, and chloramine T. Tetranitromethane and N-acetylimidazole can be used for the modification of tyrosyl residues. Cross-linking via the formation of dityrosine can be accomplished with hydrogen peroxide / copper ions. N-bromosuccinimide, 2-hydroxy-5-nitrobenzyl bromide or 3-bromo-3- methyl-2-(2-nitrophenylmercapto)-3H-indole (BPNS-skatole) have been used in recent studies for the modification of tryptophan. Peptides described herein may comprise one or more (e.g., 1, 2, 3, or 4) amino acid substitutions and / or insertions and / or deletions. Amino acid substitution means that an amino acid residue is substituted for a replacement amino acid residue at the same position. Inserted amino acid residues may be inserted at any position and may be inserted such that some or all of the inserted amino acid residues are immediately adjacent one another or may be inserted such that none of the inserted amino acid residues is immediately adjacent another inserted amino acid residue. One or more (e.g., 1, 2, 3 or 4) amino acids may be substituted and / or inserted and / or deleted from the sequence of any one of SEQ ID NOs: 30-47 and 200-240. Each substitution and / or insertion and / or deletion can take place at any position of any one of SEQ ID NOs: 30-47 and 200- 240. In some embodiments, the peptides of the disclosure may comprise additional amino acids (e.g., 1, 2, 3 or 4) at the C-terminal end and / or at the N-terminal end of the sequence of any one SEQ ID NOs: 30-47 and 200-240. A peptide of the disclosure may comprise the amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-240 except for one or more (e.g., 1, 2, 3, or 4) amino acid substitutions, insertions or deletions. Amino acid substitutions may be conservative, by which it is meant the substituted amino acid has similar chemical properties to the original amino acid. For example, the following groups of amino acids share similar chemical properties such as size, charge, and polarity: Group 1 - Ala, Ser, Thr, Pro, Gly; Group 2 - Asp, Asn, Glu, Gln; Group 3 - His, Arg, Lys; Group 4 - Met, Leu, Ile, Val, Cys; Group 5 - Phe, Thy, Trp. In another aspect, the disclosure provides a complex of a peptide of the disclosure and an MHC molecule (pMHC complex). Preferably, the peptide is bound to the peptide binding groove of the MHC molecule. In some embodiments, the peptide and the MHC molecule form a non- covalent complex. In other embodiments, the peptide and the MHC molecule may be covalentlyAttorney Docket #: 250298.000961 linked, for example, via a linker. Accordingly, the present disclosure also provides libraries comprising one or more of the pMHC complexes described herein. An exemplary pMHC complex library of the present disclosure may comprise one or more pMHC complexes comprising an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) as described herein. In some embodiments, off-target peptides associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) include those listed in Tables 2-4 herein. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) present in pMHC complexes comprises an amino acid sequence of any of SEQ ID NOs: 30-47 and 200-232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) present in pMHC complexes comprises an amino acid sequence of any of SEQ ID NOs: 200-232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) present in pMHC complexes comprises an amino acid sequence of any of SEQ ID NOs: 200-201, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) present in pMHC complexes comprises an amino acid sequence of any of SEQ ID NOs: 202-232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) present in pMHC complexes comprises an amino acid sequence of any of SEQ ID NOs: 202-230, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) present in pMHC complexes comprises an amino acid sequence of any of SEQ ID NOs: 209, 231, and 232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) present in a pMHC complex consists essentially of an amino acid sequence of any of SEQ ID NOs: 30-47 and 200-232. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) present in a pMHC complex consists essentially of an amino acid sequence of any of SEQ ID NOs: 200-232. In someAttorney Docket #: 250298.000961 embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) present in a pMHC complex consists essentially of an amino acid sequence of any of SEQ ID NOs: 200-201. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) present in a pMHC complex consists essentially of an amino acid sequence of any of SEQ ID NOs: 202-232. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) present in a pMHC complex consists essentially of an amino acid sequence of any of SEQ ID NOs: 202-230. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) present in a pMHC complex consists essentially of an amino acid sequence of any of SEQ ID NOs: 209, 231, and 232. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) present in a pMHC complex consists of an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) present in a pMHC complex consists of an amino acid sequence of any one of SEQ ID NOs: 200-232. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) present in a pMHC complex consists of an amino acid sequence of any one of SEQ ID NOs: 200-201. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) present in a pMHC complex consists of an amino acid sequence of any one of SEQ ID NOs: 202-232. In some embodiments, an off-target peptide associated with MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) present in a pMHC complex consists of an amino acid sequence of any one of SEQ ID NOs: 202-230. In some embodiments, an off-target peptide associated with MAGEA3168-176 target EVDPIGHLY (SEQ ID NO: 29) present in a pMHC complex consists of an amino acid sequence of any one of SEQ ID NOs: 209, 231, and 232. An exemplary pMHC complex library of the present disclosure may comprise one or more pMHC complexes comprising an off-target peptide associated with WT1126-134target RMFPNAPYL (SEQ ID NO: 241) as described herein. In some embodiments, off-target peptides associated with WT1126-134 target RMFPNAPYL (SEQ ID NO: 241) include those listed in Table 5 herein. In some embodiments, an off-target peptide associated with WT1126-134 target RMFPNAPYL (SEQ ID NO: 241) present in pMHC complexes comprises an amino acid sequenceAttorney Docket #: 250298.000961 of any of SEQ ID NOs: 233-240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, an off-target peptide associated with WT1126-134target RMFPNAPYL (SEQ ID NO: 241) present in a pMHC complex consists essentially of an amino acid sequence of any of SEQ ID NOs: 233-240. In some embodiments, an off-target peptide associated with WT1126-134target RMFPNAPYL (SEQ ID NO: 241) present in a pMHC complex consists of an amino acid sequence of any one of SEQ ID NOs: 233-240. pMHC complex libraries of present disclosure may comprise any number of a plurality of pMHC complexes as desired. For example, a pMHC complex library of the present disclosure may comprise at least 2 pMHC complexes, at least 3 pMHC complexes, at least 4 pMHC complexes, at least 5 pMHC complexes, at least 6 pMHC complexes, at least 7 pMHC complexes, at least 8 pMHC complexes, at least 9 pMHC complexes, at least 10 pMHC complexes, at least 20 pMHC complexes, at least 30 pMHC complexes, at least 40 pMHC complexes, at least 50 pMHC complexes, or about 2-5 pMHC complexes, about 2-10 pMHC complexes, about 5-15 pMHC complexes, about 10-20 pMHC complexes, about 10-30 pMHC complexes, about 12-25 pMHC complexes, about 20-30 pMHC complexes, about 25-50 pMHC complexes, about 40-80 pMHC complexes, about 50-100 pMHC complexes, about 60-120 pMHC complexes, about 70-140 pMHC complexes, about 80-160 pMHC complexes, about 90-180 pMHC complexes, about 100- 200 pMHC complexes, about 110-220 pMHC complexes, about 120-240 pMHC complexes, about 130-260 pMHC complexes, about 140-280 pMHC complexes, about 150-300 pMHC complexes, about 160-320 pMHC complexes, about 170-340 pMHC complexes, about 180-360 pMHC complexes, about 190-380 pMHC complexes, about 200-400 pMHC complexes, about 210-420 pMHC complexes, about 220-440 pMHC complexes, about 230-460 pMHC complexes, about 240-480 pMHC complexes, about 250-500 pMHC complexes, about 260-520 pMHC complexes, about 270-540 pMHC complexes, about 280-560 pMHC complexes, about 290-580 pMHC complexes, about 300-600 pMHC complexes, about 310-620 pMHC complexes, about 320-640 pMHC complexes, about 330-660 pMHC complexes, about 340-680 pMHC complexes, about 350-700 pMHC complexes, about 360-720 pMHC complexes, about 370-740 pMHC complexes, about 380-760 pMHC complexes, about 390-780 pMHC complexes, about 400-800 pMHC complexes, about 410-820 pMHC complexes, about 420-840 pMHC complexes, about 430-860 pMHC complexes, about 440-880 pMHC complexes, about 450-900 pMHC complexes, aboutAttorney Docket #: 250298.000961 460-920 pMHC complexes, about 470-940 pMHC complexes, about 480-960 pMHC complexes, about 490-980 pMHC complexes, about 500-1000 pMHC complexes, etc. MHC molecules used in pMHC complexes described herein include naturally occurring full-length MHC molecules as well as individual chains of MHC molecules (e.g., MHC class I α (heavy) chain, β2-microglobulin, MHC class II α chain, and MHC class II β chain), individual subunits of such chains of MHCs (e.g., α1, α2 and / or α3 subunits of MHC class I α chain, α1 and / or α2 subunits of MHC class II α chain, β1 and / or β2 subunits of MHC class II β chain) as well as fragments, mutants, and various derivatives thereof (including fusion proteins, e.g., fusions with viral envelope proteins or fusogens), wherein such fragments, mutants, and derivatives retain the ability to display an antigenic determinant for recognition by an antigen- recognition molecule. Naturally-occurring MHC molecules are encoded by a cluster of genes on human chromosome 6 or mouse chromosome 17. MHCs are also referred to as H-2 in mice and Human Leucocyte Antigen (HLA) in humans. MHC class I molecules specifically bind CD8 molecules expressed on cytotoxic T lymphocytes (CD8+ T cells), whereas MHC class II molecules specifically bind CD4 molecules expressed on helper T lymphocytes (CD4+ T cells). MHCs include, but are not limited to, HLA specificities such as A (e.g., A1-A74), B (e.g., B1-B77), C (e.g., C1-C11), D (e.g., D1-D26), E, G, DR (e.g., DR1-DR8), DQ (e.g., DQ1-DQ9) and DP (e.g., DP1-DP6). In some embodiments, the MHC molecule in a pMHC complex of the present disclosure is a human leukocyte antigen (HLA) molecule. The MHC molecule may be a human HLA molecule selected from the group consisting of HLA-A, HLA-B, HLA-C, HLA-E, HLA-F, and HLA-G. In some embodiments, the MHC class I or MHC II polypeptides may be derived from any functional human HLA-A, B, C, DR, or DQ molecules. Non-limiting examples of HLA-A alleles comprise, without limitation, A*01:01, A*02:01, A*02:02, A*03:01, A*11:01, A*23:01, A*24:02, A*25:01, A*26:01, A*29:01, A*29:02, A*31:01, A*32:01, A*33:01, A*34:01, A*36:01, A*43:01, A*66:01, A*68:01, A*69:01, A*74:01, and A*80:01. Non-limiting examples of HLA-B alleles comprise, without limitation, B*07:02. B*08:01, B*13:01, B*14:01, B*14:02, B*15:01, B*18:01, B*18:02, B*27:01, B*27:02, B*35:01, B*35:02, B*37:01, B*38:01, B*39:01, B*40:01, B*41:01, B*42:01, B*44:02, B*45:01, B*46:01, B*47:01, B*48:01, B*49:01, B*50:01, B*51:01, B*52:01, B*53:01, B*54:01, B*55:01, B*55:02, B*56:01, B*57:01, B*58:01, B*59:01, B*67:01, B*73:01, B*15:17, B*81:01, B*82:01, and B*83:01. Non-limiting examples of HLA-CAttorney Docket #: 250298.000961 alleles comprise, without limitation, C*01:01, C*02:02, C*03:03, C*04:01, C*05:01, C*06:02, C*07:01, C*07:02, C*08:02, C*12:03, C*14:01, C*15:02, C*16:01, C*17:01, and. C*18:01. Non- limiting examples of HLA-DR alleles comprise, without limitation, DRB1*01:01, DRB1*01:03, DRB1*15:01, DRB1*15:02, DRB1*16:01, DRB1*16:02, DRB1*03:01, DRB1*04:01, DRB1*04:04, DRB1*11:01, DRB1*12:01, DRB1*13:01, DRB1*13:02, DRB1*14:01, DRB1*14:02, DRB1*07:01, DRB1*08:01, DRB1*08:02, DRB1*08:03, DRB1*09:01, and DRB1*10:01. In some embodiments, the MHC class I molecule may be selected from HLA-A*02, HLA-A*01, HLA-A*03, HLA-A*11, HLA-A*23, HLA-A*24, HLA-B*07, HLA-B*08, HLA- B*40, HLA-B*44, HLA-B*15, HLA-C*04, HLA*C*03, and HLA-C*07. There are also allelic variants of the above HLA types, all of which are encompassed by the present disclosure. In some embodiments, the MHC molecule may be HLA-A*02:01 or HLA-A*01:01. Naturally occurring MHC class I molecules consist of an α (heavy) chain associated with β2-microglobulin. The heavy chain consists of subunits α1-α3. The β2-microglobulin protein and α3 subunit of the heavy chain are associated. In certain embodiments, β2-microglobulin and α3 subunit are covalently bound. In certain embodiments, β2-microglobulin and α3 subunit are non- covalently bound. The α1 and α2 subunits of the heavy chain fold to form a groove for a peptide to be displayed and recognized by TCR. In some embodiments, the MHC contained in a pMHC complex of the disclosure comprises (i) a class I MHC polypeptide or a fragment, mutant or derivative thereof, and, optionally, (ii) a β2 microglobulin polypeptide or a fragment, mutant or derivative thereof. In one specific embodiment, the class I MHC polypeptide is linked to the β2 microglobulin polypeptide by a peptide linker. pMHC complexes of the disclosure may be isolated and / or in a substantially pure form. For example, the complex may be provided in a form which is substantially free of other peptides or proteins. MHC molecules as disclosed herein can include recombinant MHC molecules, non- naturally occurring MHC molecules, and functionally equivalent fragments of MHC, including derivatives or variants thereof, provided that peptide binding is retained. For example, MHC molecules may be attached to a solid support, in soluble form, attached to a tag, biotinylated and / or in multimeric form. A peptide disclosed herein may be covalently attached to the MHC.Attorney Docket #: 250298.000961 Methods to produce soluble recombinant MHC molecules with which peptides disclosed herein can form a complex include, but are not limited to, expression and purification from E. coli cells or insect cells. Alternatively, MHC molecules may be produced synthetically, or using cell free systems. The peptides disclosed herein may be presented on the surface of a cell in complex with MHC. Thus, the present disclosure also provides a cell presenting on its surface a pMHC complex disclosed herein. Such a cell may be a mammalian cell, preferably a cell of the immune system, and a specialized antigen-presenting cell (APC) such as a dendritic cell or a B cell. The cell may be an immortalized cell. The cell may be a cell that does not naturally present the peptide of interest. In certain embodiments, the cell may be a cell that is deficient in presenting endogenous peptides in complex with MHC on the cell surface. For example, the cell may be a cell that has been genetically modified to be deficient in endogenous peptide presentation, such as a cell that has been modified to be transporter associated with antigen processing (TAP) deficient. The cell may be a cell that requires loading exogenous peptide on the cell surface in order to measurably detect antigen-recognition molecule binding to the peptide. Incubation of the cell with exogenous β2 microglobulin (β2m) may increase the loading / presentation of exogenously administered peptides. Preferred cells may include T2 cells, which are well known in the art. See, e.g., Elliot et al., J Exp Med. 1995 Apr 1;181(4):1481-91, which is herein incorporated by reference in its entirety. Cells presenting a peptide or pMHC complex of the disclosure may be isolated, preferably in the form of a homogenous population, or provided in a substantially pure form. Such cells may not naturally present a pMHC complex of the disclosure, or alternatively said cells may present the pMHC complex at a level higher than they would in nature. Cells presenting pMHC complexes may be obtained by pulsing said cells with one or more peptides (e.g., 2 to 10, 2 to 20, 2 to 30, 5 to 25, 5 to 20, or 10 to 15 peptides) of the disclosure, or genetically modifying the cells (via DNA or RNA transfer) to express one or more peptides (e.g., 2 to 10, 2 to 20, 2 to 30, 5 to 25, 5 to 20, or 10 to 15 peptides) of the disclosure. Pulsing involves incubating the cells with the peptide for several hours using peptide concentrations typically ranging from 10−5to 10−12M. Pulsing may also involve incubating the cells with exogenous β2m molecules, for example at the same or in similar concentrations as the peptide. Such cells may additionally be transduced with HLA molecules, such as HLA-A*02 to further induce presentation of the peptide(s). Cells may beAttorney Docket #: 250298.000961 produced recombinantly. Cells presenting peptides of the disclosure may be used to isolate antigen-binding molecules (e.g., antibodies, T cells, TCRs and CARs) which can bind to the cells. Peptides or pMHC complexes disclosed herein may be fused or conjugated to one or more heterologous molecules. Peptides or pMHC complexes of the disclosed herein may also be in multimeric form. Accordingly, the present disclosure also provides fusion proteins, conjugates, and oligomeric complexes comprising a peptide or a pMHC complex of the disclosure. In some embodiments, peptides are fused or conjugated to one or more heterologous molecules which can include an MHC molecule (or fragments thereof). Heterologous molecules suitable for genetical fusion and / or chemical conjugation with the peptides or the pMHC complexes of the disclosure include, but are not limited to, peptides, polypeptides, small molecules, polymers, nucleic acids, lipids, sugars, etc. The heterologous molecule(s) may be fused at the N- and / or C-terminus of the peptide and / or another polypeptide chain in the pMHC complex. Heterologous peptides and polypeptides include, but are not limited to, an epitope (e.g., FLAG) or a tag sequence (e.g., His6(SEQ ID NO: 149), and the like) to allow for the detection and / or isolation of a fusion protein; a transmembrane receptor protein or a portion thereof, such as an extracellular domain or a transmembrane and intracellular domain; a ligand or a portion thereof which binds to a transmembrane receptor protein; an enzyme or portion thereof which is catalytically active; a polypeptide or peptide which promotes oligomerization, such as a leucine zipper domain; a polypeptide or peptide which increases stability, such as an immunoglobulin constant region (e.g., an Fc domain); a half-life-extending sequence comprising a combination of two or more (e.g., 2, 5, 10, 15, 20, 25, etc.) naturally occurring or non-naturally occurring charged and / or uncharged amino acids (e.g., Ser, Gly, Glu or Asp) designed to form a predominantly hydrophilic or predominantly hydrophobic fusion partner for a fusion protein; a functional or non- functional antibody (e.g., an antibody that is specific for dendritic cells), or a heavy or light chain thereof; and a polypeptide which has an activity different from fusion proteins of the present disclosure. In some embodiments, fusion proteins of the disclosure may comprise one or more affinity tags, e.g., to allow for affinity purification or coupling to another molecule. Examples of affinity tags include, but are not limited to, a His6 (SEQ ID NO: 149) tag, an Avi-tag, a biotin, a hemagglutinin (HA) tag, a FLAG tag, a Myc tag, a GST tag, a MBP tag, a chitin binding proteinAttorney Docket #: 250298.000961 tag, a calmodulin tag, a V5 tag, a streptavidin binding tag, a green fluorescent protein (GFP), YFP, RFP, CFP, mCherry, tdTomato, SUMO tag, and Ubiquitin tag. Peptides or pMHC complexes of the disclosure may be provided in soluble form, or may be immobilized by attachment to a suitable solid support. Examples of solid supports include, but are not limited to, a bead (e.g., a magnetic bead), a membrane, sepharose, a plate, a tube, a column, etc. pMHC complexes may be attached, for example, to an ELISA plate, a magnetic bead, or a surface plasmon resonance biosensor chip. Methods of attaching peptides or pMHC complexes to a solid support are known to the skilled person, and include, for example, using an affinity binding pair, e.g., biotin and streptavidin, or antibodies and antigens. In some embodiments, peptides or pMHC complexes are labeled with biotin and attached to streptavidin-coated surfaces. In another aspect, the disclosure provides an isolated polynucleotide comprising a nucleic acid sequence encoding one or more peptide(s) and / or peptide-based molecules (such as complexes (e.g., pMHC complexes), fusion proteins, or conjugates comprising the described peptides) of the disclosure. The polynucleotide may be, for example, DNA, cDNA, PNA, RNA or combinations thereof, either single- and / or double-stranded, or native or stabilized forms of polynucleotides, such as, for example, polynucleotides with a phosphorothioate backbone and it may or may not contain introns so long as it codes for the peptide. In some embodiments, a polynucleotide described herein encodes a peptide comprising an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232, or a fragment or derivative thereof. In some embodiments, the polynucleotide described herein encodes a peptide consisting essentially of an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232, or a fragment or derivative thereof. In some embodiments, the polynucleotide described herein encodes a peptide consisting of an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232, or a fragment or derivative thereof. In some embodiments, a polynucleotide described herein encodes a peptide comprising an amino acid sequence of any one of SEQ ID NOs: 200-232, or a fragment or derivative thereof. In some embodiments, the polynucleotide described herein encodes a peptide consisting essentially of an amino acid sequence of any one of SEQ ID NOs: 200-232, or a fragment or derivative thereof. In some embodiments, the polynucleotide described herein encodes a peptide consisting of an amino acid sequence of any one of SEQ ID NOs: 200-232, or a fragment or derivative thereofAttorney Docket #: 250298.000961 In some embodiments, a polynucleotide described herein encodes a peptide comprising an amino acid sequence of any one of SEQ ID NOs: 200-201, or a fragment or derivative thereof. In some embodiments, the polynucleotide described herein encodes a peptide consisting essentially of an amino acid sequence of any one of SEQ ID NOs: 200-201, or a fragment or derivative thereof. In some embodiments, the polynucleotide described herein encodes a peptide consisting of an amino acid sequence of any one of SEQ ID NOs: 200-201, or a fragment or derivative thereof. In some embodiments, a polynucleotide described herein encodes a peptide comprising an amino acid sequence of SEQ ID NOs: 202-232, or a fragment or derivative thereof. In some embodiments, the polynucleotide described herein encodes a peptide consisting essentially of an amino acid sequence of SEQ ID NOs: 202-232, or a fragment or derivative thereof. In some embodiments, the polynucleotide described herein encodes a peptide consisting of an amino acid sequence of SEQ ID NOs: 202-232, or a fragment or derivative thereof. In some embodiments, a polynucleotide described herein encodes a peptide comprising an amino acid sequence of SEQ ID NOs: 202-230, or a fragment or derivative thereof. In some embodiments, the polynucleotide described herein encodes a peptide consisting essentially of an amino acid sequence of SEQ ID NOs: 202-230, or a fragment or derivative thereof. In some embodiments, the polynucleotide described herein encodes a peptide consisting of an amino acid sequence of SEQ ID NOs: 202-230, or a fragment or derivative thereof. In some embodiments, a polynucleotide described herein encodes a peptide comprising an amino acid sequence of SEQ ID NOs: 209, 231, and 232, or a fragment or derivative thereof. In some embodiments, the polynucleotide described herein encodes a peptide consisting essentially of an amino acid sequence of SEQ ID NOs: 209, 231, and 232, or a fragment or derivative thereof. In some embodiments, the polynucleotide described herein encodes a peptide consisting of an amino acid sequence of SEQ ID NOs: 209, 231, and 232, or a fragment or derivative thereof. In some embodiments, a polynucleotide described herein encodes a peptide comprising an amino acid sequence of SEQ ID NOs: 233-240, or a fragment or derivative thereof. In some embodiments, the polynucleotide described herein encodes a peptide consisting essentially of an amino acid sequence of SEQ ID NOs: 233-240, or a fragment or derivative thereof. In someAttorney Docket #: 250298.000961 embodiments, the polynucleotide described herein encodes a peptide consisting of an amino acid sequence of SEQ ID NOs: 233-240, or a fragment or derivative thereof. In a further aspect, the disclosure provides a vector comprising a nucleic acid sequence of the disclosure. The vector may include, in addition to a nucleic acid sequence encoding only a peptide of the disclosure, one or more additional nucleic acid sequences encoding one or more additional peptides. Such additional peptides may, once expressed, be fused to the N-terminus or the C-terminus of the peptide of the disclosure. Examples of such additional peptides are detailed in the sections above. In one embodiment, the vector includes a nucleic acid sequence encoding a peptide or protein tag such as, for example, a biotinylation site, a FLAG-tag, a MYC-tag, an HA- tag, a GST-tag, a Strep-tag or a poly-histidine tag. The off-target peptides identified herein may be used for evaluation and / or screening of therapeutic molecules for molecules that have minimal off-target effects. Such therapeutic molecules can include antigen-recognition molecules such as T cell Receptors (TCRs), chimeric antigen receptors (CARs), and antibodies or antigen-binding fragments thereof. In various embodiments of the present disclosure, the antigen-recognition molecule is present in a solution. In various embodiments of the present disclosure, the antigen-recognition molecule is present on a cell (e.g., T cell, B cell or hybridoma). In certain embodiments, the antigen-recognition molecule is present on a heterologous cell. For example, a heterologous host cell may be genetically modified to express the antigen recognition molecule as is known in the art. In one aspect, the disclosure provides an in vitro method of assessing off-target effects of an antigen-recognition molecule, said method comprising a) contacting the antigen-recognition molecule with a target peptide presented in a complex with a major histocompatibility complex (MHC) molecule (MHC-target peptide complex); b) contacting the antigen-recognition molecule with one or more off-target peptides associated with said target peptide, wherein each of said off- target peptides is presented in a complex with the same MHC molecule as in a) (MHC-off-target peptide complex); and c) determining and comparing the level of binding of the antigen- recognition molecule to MHC-target peptide complex and each of the MHC-off-target peptide complexes. In one aspect, the disclosure provides an in vitro method of assessing off-target effects of an antigen-recognition molecule, comprising a) contacting the antigen-recognition molecule with one or more off-target peptides associated with a target peptide that is recognized by the antigen-Attorney Docket #: 250298.000961 recognition molecule, wherein each of said off-target peptides is presented in a complex with a major histocompatibility complex (MHC) molecule (MHC-off-target peptide complex); and b) determining the level of binding of the antigen-recognition molecule to each of the MHC-off-target peptide complexes. In one aspect, the disclosure provides an in vitro method of assessing off-target effects of an antigen-recognition molecule that targets MAGEA3168-176 and / or WT1126-134 peptide, comprising a) contacting the antigen-recognition molecule with MAGEA3168-176 and / or WT1126-134peptide presented in a complex with a major histocompatibility complex (MHC) molecule, or a fragment or derivative thereof (MHC-MAGEA3168-176 and / or MHC-WT1126-134 peptide complex); b) contacting the antigen-recognition molecule with one or more off-target peptides, wherein each of said off-target peptides (i) comprises an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232 and / or 233-240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof, wherein the peptide is 8-12 amino acids in length, and (ii) is presented in a complex with the same kind of MHC molecule, or the fragment or derivative thereof, as in (a) (MHC-off-target peptide complex); and c) determining the level of binding of the antigen- recognition molecule to the MHC-MAGEA3168-176 and / or MHC-WT1126-134 peptide complex and each of the MHC-off-target peptide complexes. In one aspect, the disclosure provides an in vitro method of assessing off-target effects of an antigen-recognition molecule that targets MAGEA3168-176 and / or WT1126-134 peptide, comprising a) contacting the antigen-recognition molecule with MAGEA3168-176 and / or WT1126-134peptide presented in a complex with a major histocompatibility complex (MHC) molecule, or a fragment or derivative thereof (MHC-MAGEA3168-176and / or MHC-WT1126-134peptide complex); b) contacting the antigen-recognition molecule with one or more off-target peptides, wherein each of said off-target peptides (i) comprises an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232 and / or 233-240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof, wherein the peptide is 8-12 amino acids in length, and (ii) is presented in a complex with the same kind of MHC molecule, or the fragment or derivative thereof, as in (a) (MHC-off-target peptide complex); and c) determining the binding affinity of the antigen- recognition molecule to the MHC-MAGEA3168-176 and / or MHC-WT1126-134 peptide complex and each of the MHC-off-target peptide complexes.Attorney Docket #: 250298.000961 In one aspect, the disclosure provides an in vitro method of assessing off-target effects of an antigen-recognition molecule that targets MAGEA3168-176and / or WT1126-134, comprising a) contacting the antigen-recognition molecule with one or more off-target peptides, wherein each of said off-target peptides comprises an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232 and / or 233-240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof, wherein the peptide is 8-12 amino acids in length, and wherein each of said off-target peptides is presented in one of the following forms: (1) as a complex with a major histocompatibility complex (MHC) molecule, or a fragment or derivative thereof (MHC-off-target peptide complex), (2) as a peptide, or (3) as a protein or fragment thereof comprising said peptide; and b) determining the level of binding of the antigen-recognition molecule to said one or more MHC-off-target peptide complexes, off-target peptides or proteins or fragments thereof comprising said off-target peptides. In one aspect, the disclosure provides an in vitro method of assessing off-target effects of an antigen-recognition molecule that targets MAGEA3168-176and / or WT1126-134, comprising a) contacting the antigen-recognition molecule with one or more off-target peptides, wherein each of said off-target peptides comprises an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232 and / or 233-240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof, wherein the peptide is 8-12 amino acids in length, and wherein each of said off-target peptides is presented in one of the following forms: (1) as a complex with a major histocompatibility complex (MHC) molecule, or a fragment or derivative thereof (MHC-off-target peptide complex), (2) as a peptide, or (3) as a protein or fragment thereof comprising said peptide; and b) determining the binding affinity of the antigen-recognition molecule to said one or more MHC-off-target peptide complexes, off-target peptides or proteins or fragments thereof comprising said off-target peptides. In some embodiments of the above-described in vitro methods of assessing off-target effects of an antigen-recognition molecule that targets MAGEA3168-176, the MAGEA3168-176 peptide comprises the amino acid sequence of EVDPIGHLY (SEQ ID NO: 29) . In some embodiments of the in vitro methods, the MAGEA3168-176peptide consists of the amino acid sequence EVDPIGHLY (SEQ ID NO: 29). In some embodiments of the above-described in vitro methods of assessing off-target effects of an antigen-recognition molecule that targets MAGEA3168-176, the off-target peptideAttorney Docket #: 250298.000961 comprises an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232. In some embodiments of the in vitro methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232. In some embodiments of the above-described in vitro methods of assessing off-target effects of an antigen-recognition molecule that targets MAGEA3168-176, the off-target peptide comprises an amino acid sequence of any one of SEQ ID NOs: 200-232. In some embodiments of the in vitro methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 200-232. In some embodiments of the above-described in vitro methods of assessing off-target effects of an antigen-recognition molecule that targets MAGEA3168-176, the off-target peptide comprises an amino acid sequence of any one of SEQ ID NOs: 200-201. In some embodiments of the in vitro methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 200-201. In some embodiments of the above-described in vitro methods of assessing off-target effects of an antigen-recognition molecule that targets MAGEA3168-176, the off-target peptide comprises an amino acid sequence of SEQ ID NO: 202-232. In some embodiments of the in vitro methods, the off-target peptide consists of an amino acid sequence of SEQ ID NO: 202-232. In some embodiments of the above-described in vitro methods of assessing off-target effects of an antigen-recognition molecule that targets MAGEA3168-176, the off-target peptide comprises an amino acid sequence of SEQ ID NO: 202-230. In some embodiments of the in vitro methods, the off-target peptide consists of an amino acid sequence of SEQ ID NO: 202-230. In some embodiments of the above-described in vitro methods of assessing off-target effects of an antigen-recognition molecule that targets MAGEA3168-176, the off-target peptide comprises an amino acid sequence of SEQ ID NO: 209, 231, and 232. In some embodiments of the in vitro methods, the off-target peptide consists of an amino acid sequence of SEQ ID NO: 209, 231, and 232. In some embodiments of the above-described in vitro methods of assessing off-target effects of an antigen-recognition molecule that targets WT1126-134, the WT1126-134peptide comprises the amino acid sequence of RMFPNAPYL (SEQ ID NO: 241) . In some embodiments of the in vitro methods, the WT1126-134 peptide consists of the amino acid sequence RMFPNAPYL (SEQ ID NO: 241).Attorney Docket #: 250298.000961 In some embodiments of the above-described in vitro methods of assessing off-target effects of an antigen-recognition molecule that targets WT1126-134, the off-target peptide comprises an amino acid sequence of any one of SEQ ID NOs: 233-240. In some embodiments of the in vitro methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 233-240. In some embodiments of the in vitro methods described above, the level of binding is determined by detecting the amount of antigen-recognition molecules bound to the MHC-peptide complexes. For example, if a signal correlated to binding of an antigen-recognition molecule to an MHC peptide complex has a S:N ratio of at least about 2.0, 2.5, 3.0, 3.5, 4.0, or 5.0 then the antigen-recognition molecule may be determined to exhibit detectable binding to the MHC peptide complex. Noise levels (N) may be determined, for example, by measuring a signal / level of binding to a cell with no peptide and / or with no primary / capture antibody / agent (i.e., with only a detection antibody / agent). If an antigen-recognition molecule specifically binds to one or more MHC-off- target peptide complexes, then the antigen-recognition molecule may exhibit off-target effects. In some specific embodiments, a S:N ratio of at least about 3 is indicative of detectable binding. In some embodiments, binding affinity may be determined. Binding affinity may be determined by measuring an equilibrium dissociation constant (KD) of the binding reaction. Alternatively, binding affinity may be characterized using other methods. In some embodiments, the in vitro methods include determining that the antigen- recognition molecule is likely to have off-target effects if it detectably binds to at least one MHC- off-target peptide complex, wherein the off-target peptide is expressed in essential, normal tissues. In some embodiments, the in vitro methods include determining that the antigen-recognition molecule is likely to have off-target effects if it detectably binds to at least one MHC-off-target peptide complex, wherein the off-target peptide is expressed in diseased tissues. In some embodiments, the in vitro methods include determining that an antigen- recognition molecule is likely to have off-target effects if it detectably binds to at least one MHC- off-target peptide complex, off-target peptide or protein or fragment thereof, comprising said off- target peptide. In some embodiments, the antigen-recognition molecule is likely to have off-target effects if it detectably binds to at least one MHC-off-target peptide complex, or off-target peptideAttorney Docket #: 250298.000961 or protein or fragment thereof comprising said off-target peptide, when the off-target peptide is present on a surface of a cell at a copy number of at least about 500 to about 10,000 copies / cell. In some embodiments, the antigen-recognition molecule is likely to have off-target effects if it detectably binds to at least one MHC-off-target peptide complex, or off-target peptide or protein or fragment thereof comprising said off-target peptide, when the off-target peptide is present on a surface of a cell at a copy number of at least about 500, at least about 600, at least about 700, at least about 800, or at least about 900 copies / cell. In some embodiments, the antigen-recognition molecule is likely to have off-target effects if it detectably binds to at least one MHC-off-target peptide complex, or off-target peptide or protein or fragment thereof comprising said off-target peptide, when the off-target peptide is present on a surface of a cell at a copy number of at least about 1,000, at least about 2,000, at least about 3,000, at least about 4,000, at least about 5,000, at least about 6,000, at least about 7,000, at least about 8,000, at least about 9,000, or at least about 10,000 copies / cell. In some embodiments, the antigen-recognition molecule is likely to have off-target effects if it detectably binds to at least one MHC-off-target peptide complex, or off-target peptide or protein or fragment thereof comprising said off-target peptide, when the off-target peptide is present on a surface of a cell at a copy number of at least about at least about 550 to about 9,800, at least about 600 to about 9,600, at least about 650 to about 9,400, at least about 700 to about 9,200, at least about 750 to about 9,000, at least about 800 to about 8,800, at least about 850 to about 8,600, at least about 900 to about 8,400, at least about 950 to about 8,200, at least about 1000 to about 8,000, at least about 1,050 to about 7,800, at least about 1,100 to about 7,600, at least about 1,150 to about 7,400, at least about 1,200 to about 7,200, at least about 1,250 to about 7,000, at least about 1,300 to about 6,800, at least about 1,350 to about 6,600, at least about 1,400 to about 6,400, at least about 1,450 to about 6,200, or at least about 1,500 to about 6,000 copies / cell. In some embodiments, the antigen-recognition molecule is likely to have off-target effects if it detectably binds to at least one MHC-off-target peptide complex, or off-target peptide or protein or fragment thereof comprising said off-target peptide, when the off-target peptide is present on a surface of a cell at a copy number of at least about 1,000 to about 10,000, at least about 1,000 to about 9,500, at least about 1,000 to about 9,000, at least about 1,000 to about 8,500, at least about 1,000 to about 8,000, at least about 1,000 to about 7,500, at least about 1,000 to aboutAttorney Docket #: 250298.000961 7,000, at least about 1,000 to about 6,500, at least about 1,000 to about 6,000, at least about 1,000 to about 5,500, at least about 1,000 to about 5,000, at least about 1,000 to about 4,500, at least about 1,000 to about 4,000, at least about 1,000 to about 3,500, at least about 1,000 to about 3,000, at least about 1,000 to about 2,500, at least about 1,000 to about 2,000, or at least about 1,000 to about 1,500 copies / cell. In some embodiments, the antigen-recognition molecule is likely to have off-target effects if it detectably binds to at least one MHC-off-target peptide complex, or off-target peptide or protein or fragment thereof comprising said off-target peptide, when the off-target peptide is present on a surface of a cell at a copy number of at least about 1,000, at least about 1,010, at least about 1,020, at least about 1,030, at least about 1,040, at least about 1,050, at least about 1,100, at least about 1,150, at least about 1,200, at least about 1,250, at least about 1,300, at least about 1,350, at least about 1,400, at least about 1,450, at least about 1,500, at least about 1,550, at least about 1,600, at least about 1,650, at least about 1,700, at least about 1,750, at least about 1,800, at least about 1,850, at least about 1,900, at least about 1,950, or at least about 2,000 copies / cell. In some embodiments, the antigen-recognition molecule is likely to have off-target effects if it detectably binds to at least one MHC-off-target peptide complex, or off-target peptide or protein or fragment thereof comprising said off-target peptide, when the off-target peptide is present on a surface of a cell at a copy number of at least about 1,000 copies / cell. In another aspect, the disclosure provides a method of selecting an antigen-recognition molecule that binds a target pMHC complex with minimal off-target effects. Such method can comprise a) contacting a plurality of antigen-recognition molecules with a target peptide presented in a complex with a major histocompatibility complex (MHC) molecule (MHC-target peptide complex); b) contacting the same plurality of antigen-recognition molecules with one or more off- target peptides associated with said target peptide, wherein each of said off-target peptides is presented in a complex with the same MHC molecule as in a) (MHC-off-target peptide complex); c) selecting one or more antigen-recognition molecules based at least in part on the number of MHC-off-target peptide complexes detectably bound by each of the antigen-recognition molecules; and d) optionally, repeating steps (a)-(c) using selected antigen-recognition molecules. In some embodiments, the method includes selecting the antigen-recognition molecule(s) that binds to the fewest MHC-off-target peptide complexes. In some embodiments, the selected antigen-recognition molecule(s) detectably bind no more than five (e.g., no more than four, noAttorney Docket #: 250298.000961 more than three, no more than two, or no more than one) MHC-off-target peptide complexes, wherein the off-target peptides are expressed in essential, normal tissues. In some embodiments, the selected antigen-recognition molecule(s) do not detectably bind to any of the MHC-off-target peptide complexes, wherein the off-target peptides are expressed in essential, normal tissues. In some embodiments, if several selected antigen-recognition molecules bind to at least one MHC-off-target peptide complex, the method may also include a step of comparing the level of binding of the antigen-recognition molecule(s) to the MHC-target peptide complex versus to the MHC-off-target peptide complex(es). The antigen-recognition molecule(s) may likely bind to the MHC-target peptide complex stronger than to the MHC-off-target peptide complex(es). For example, the antigen-recognition molecule(s) may bind to the MHC-target peptide complex about 1000 times, about 500 times, about 200 times, about 100 times, about 90 times, about 80 times, about 70 times, about 60 times, about 50 times, about 40 times, about 30 times, about 20 times, or about 10 times stronger than to the MHC-off-target peptide complex(es). The method may further include selecting the antigen-recognition molecule(s) based at least in part on the MHC-target peptide complex / MHC-off-target peptide complex binding ratio for one or more off-target peptides, wherein a higher MHC-target peptide complex / MHC-off-target peptide complex binding ratio is more desirable. In some embodiments, selection of antigen-recognition molecules may take into consideration the level of binding of the plurality of antigen-recognition molecules to the MHC- target peptide complex, wherein stronger binding to the MHC-target peptide complex is more desirable. Accordingly, the method may include selecting the antigen-recognition molecule(s) based at least in part on the level of binding to the MHC-target peptide complex. In some embodiments, the selected antigen-recognition molecules(s) bind to at least one potential secondary target peptide in addition to the MHC-target peptide complex. In another aspect, the disclosure provides a method for selecting an antigen-recognition molecule that targets MAGEA3168-176and / or WT1126-134peptide, comprising a) contacting a plurality of antigen-recognition molecules with MAGEA3168-176and / or WT1126-134peptide presented in a complex with a major histocompatibility complex (MHC) molecule, or a fragment or derivative thereof (MHC-MAGEA3168-176 and / or MHC-WT1126-134peptide complex) or presented as MAGEA3168-176and / or WT1126-134peptide or MAGEA3 and / or WT1 protein orAttorney Docket #: 250298.000961 fragment thereof comprising said MAGEA3168-176and / or WT1126-134peptide; b) contacting the same plurality of antigen-recognition molecules with one or more off-target peptides, (i) wherein each of said off-target peptides comprises an amino acid sequence of any one of SEQ ID NOs: 30- 47 and 200-232 and / or 233-240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof, wherein the peptide is 8-12 amino acids in length, and (ii) wherein each of said off-target peptides is presented in one of the following forms: (1) as a complex with the same kind of MHC molecule, or the fragment or derivative thereof as in (a) (MHC-off-target peptide complex), (2) as a peptide, or (3) as a protein or fragment thereof comprising said off-target peptide; c) selecting one or more antigen-recognition molecules based on their ability to detectably bind to MAGEA3168-176 and / or WT1126-134 peptide complex or MAGEA3168-176 and / or WT1126-134 peptide or MAGEA3 and / or WT1 protein or fragment thereof comprising said MAGEA3168-176and / or WT1126-134peptide and based at least in part on the number of MHC-off-target peptide complexes, off-target peptides or proteins or fragments thereof comprising said off-target peptides detectably bound by each of the antigen-recognition molecules; and d) optionally, repeating steps (a)-(c) using the one or more selected antigen-recognition molecules. In another aspect, the disclosure provides a method for selecting an antigen-recognition molecule that specifically binds MAGEA3168-176 and / or WT1126-134 peptide, comprising a) contacting a plurality of antigen-recognition molecules with MAGEA3168-176and / or WT1126-134peptide presented in a complex with a major histocompatibility complex (MHC) molecule, or a fragment or derivative thereof (MHC-MAGEA3168-176 and / or MHC-WT1126-134 peptide complex) or presented as MAGEA3168-176and / or WT1126-134peptide or MAGEA3 and / or WT1 protein or fragment thereof comprising said MAGEA3168-176and / or WT1126-134peptide; b) contacting the same plurality of antigen-recognition molecules with one or more off-target peptides, (i) wherein each of said off-target peptides comprises an amino acid sequence of any one of SEQ ID NOs: 30- 47 and 200-232 and / or 233-240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof, wherein the peptide is 8-12 amino acids in length, and (ii) wherein each of said off-target peptides is presented in one of the following forms: (1) as a complex with the same kind of MHC molecule, or the fragment or derivative thereof as in (a) (MHC-off-target peptide complex), (2) as a peptide, or (3) as a protein or fragment thereof comprising said off-target peptide; c) selecting one or more antigen-recognition molecules based on their ability to detectably bind to MAGEA3168-176and / or WT1126-134peptide complex or MAGEA3168-176and / or WT1126-134Attorney Docket #: 250298.000961 peptide or MAGEA3 and / or WT1 protein or fragment thereof comprising said MAGEA3168-176and / or WT1126-134peptide and based at least in part on the number of MHC-off-target peptide complexes, off-target peptides or proteins or fragments thereof comprising said off-target peptides detectably bound by each of the antigen-recognition molecules; and d) optionally, repeating steps (a)-(c) using the one or more selected antigen-recognition molecules. In some embodiments of the above-described methods for selecting an antigen- recognition molecule that targets MAGEA3168-176 peptide, the MAGEA3168-176 peptide comprises the amino acid sequence of EVDPIGHLY (SEQ ID NO: 29). In some embodiments of the selecting methods, the MAGEA3168-176peptide consists of the amino acid sequence EVDPIGHLY (SEQ ID NO: 29). In some embodiments of the above-described methods for selecting an antigen- recognition molecule that targets MAGEA3168-176peptide, the off-target peptide comprises an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232. In some embodiments of the selecting methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232. In some embodiments of the above-described methods for selecting an antigen- recognition molecule that targets MAGEA3168-176 peptide, the off-target peptide comprises an amino acid sequence of any one of SEQ ID NOs: 200-232. In some embodiments of the selecting methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 200-232. In some embodiments of the above-described methods for selecting an antigen- recognition molecule that targets MAGEA3168-176peptide, the off-target peptide comprises an amino acid sequence of any one of SEQ ID NOs: 200-201. In some embodiments of the selecting methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 200-201. In some embodiments of the above-described methods for selecting an antigen- recognition molecule that targets MAGEA3168-176peptide, the off-target peptide comprises an amino acid sequence of SEQ ID NO: 202-232. In some embodiments of the selecting methods, the off-target peptide consists of an amino acid sequence of SEQ ID NO: 202-232. In some embodiments of the above-described methods for selecting an antigen- recognition molecule that targets MAGEA3168-176peptide, the off-target peptide comprises anAttorney Docket #: 250298.000961 amino acid sequence of SEQ ID NO: 202-230. In some embodiments of the selecting methods, the off-target peptide consists of an amino acid sequence of SEQ ID NO: 202-230. In some embodiments of the above-described methods for selecting an antigen- recognition molecule that targets MAGEA3168-176peptide, the off-target peptide comprises an amino acid sequence of SEQ ID NO: 209, 231, and 232. In some embodiments of the selecting methods, the off-target peptide consists of an amino acid sequence of SEQ ID NO: 209, 231, and 232. In some embodiments of the above-described methods for selecting an antigen- recognition molecule that targets WT1126-134 peptide, the WT1126-134 peptide comprises the amino acid sequence of RMFPNAPYL (SEQ ID NO: 241). In some embodiments of the selecting methods, the WT1126-134peptide consists of the amino acid sequence RMFPNAPYL (SEQ ID NO: 241). In some embodiments of the above-described methods for selecting an antigen- recognition molecule that targets WT1126-134peptide, the off-target peptide comprises an amino acid sequence of any one of SEQ ID NOs: 233-240. In some embodiments of the selecting methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 233-240. In some embodiments of the above-described methods for selecting an antigen- recognition molecule that specifically binds MAGEA3168-176 and / or WT1126-134 peptide, each of said one or more off-target peptides is presented as an MHC-off-target peptide complex, or a fragment or derivative thereof, on a surface of a cell at a copy number of at least about 500 to about 10,000 copies / cell. In some embodiments of the above-described methods for selecting an antigen- recognition molecule that specifically binds MAGEA3168-176and / or WT1126-134peptide, each of said one or more off-target peptides is presented as an MHC-off-target peptide complex, or a fragment or derivative thereof, on a surface of a cell at a copy number of at least about 500, at least about 600, at least about 700, at least about 800, or at least about 900 copies / cell. In some embodiments of the above-described methods for selecting an antigen- recognition molecule that specifically binds MAGEA3168-176 and / or WT1126-134 peptide, each of said one or more off-target peptides is presented as an MHC-off-target peptide complex, or a fragment or derivative thereof, on a surface of a cell at a copy number of at least about 1,000, atAttorney Docket #: 250298.000961 least about 2,000, at least about 3,000, at least about 4,000, at least about 5,000, at least about 6,000, at least about 7,000, at least about 8,000, at least about 9,000, or at least about 10,000 copies / cell. In some embodiments of the above-described methods for selecting an antigen- recognition molecule that specifically binds MAGEA3168-176and / or WT1126-134peptide, each of said one or more off-target peptides is presented as an MHC-off-target peptide complex, or a fragment or derivative thereof, on a surface of a cell at a copy number of a cell at a copy number of at least about at least about 550 to about 9,800, at least about 600 to about 9,600, at least about 650 to about 9,400, at least about 700 to about 9,200, at least about 750 to about 9,000, at least about 800 to about 8,800, at least about 850 to about 8,600, at least about 900 to about 8,400, at least about 950 to about 8,200, at least about 1000 to about 8,000, at least about 1,050 to about 7,800, at least about 1,100 to about 7,600, at least about 1,150 to about 7,400, at least about 1,200 to about 7,200, at least about 1,250 to about 7,000, at least about 1,300 to about 6,800, at least about 1,350 to about 6,600, at least about 1,400 to about 6,400, at least about 1,450 to about 6,200, or at least about 1,500 to about 6,000 copies / cell. In some embodiments of the above-described methods for selecting an antigen- recognition molecule that specifically binds MAGEA3168-176 and / or WT1126-134peptide, each of said one or more off-target peptides is presented as an MHC-off-target peptide complex, or a fragment or derivative thereof, on a surface of a cell at a copy number of at least about 1,000 to about 10,000, at least about 1,000 to about 9,500, at least about 1,000 to about 9,000, at least about 1,000 to about 8,500, at least about 1,000 to about 8,000, at least about 1,000 to about 7,500, at least about 1,000 to about 7,000, at least about 1,000 to about 6,500, at least about 1,000 to about 6,000, at least about 1,000 to about 5,500, at least about 1,000 to about 5,000, at least about 1,000 to about 4,500, at least about 1,000 to about 4,000, at least about 1,000 to about 3,500, at least about 1,000 to about 3,000, at least about 1,000 to about 2,500, at least about 1,000 to about 2,000, or at least about 1,000 to about 1,500 copies / cell. In some embodiments of the above-described methods for selecting an antigen- recognition molecule that specifically binds MAGEA3168-176and / or WT1126-134peptide, each of said one or more off-target peptides is presented as an MHC-off-target peptide complex, or a fragment or derivative thereof, on a surface of a cell at a copy number of at least about 1,000, at least about 1,010, at least about 1,020, at least about 1,030, at least about 1,040, at least aboutAttorney Docket #: 250298.000961 1,050, at least about 1,100, at least about 1,150, at least about 1,200, at least about 1,250, at least about 1,300, at least about 1,350, at least about 1,400, at least about 1,450, at least about 1,500, at least about 1,550, at least about 1,600, at least about 1,650, at least about 1,700, at least about 1,750, at least about 1,800, at least about 1,850, at least about 1,900, at least about 1,950, or at least about 2,000 copies / cell. In some embodiments of the above-described methods for selecting an antigen- recognition molecule that specifically binds MAGEA3168-176 and / or WT1126-134 peptide, each of said one or more off-target peptides is presented as an MHC-off-target peptide complex, or a fragment or derivative thereof, on a surface of a cell at a copy number of at least about 1,000 copies / cell. In some embodiments, the one or more selected antigen-recognition molecules detectably bind no more than five MHC-off-target peptide complexes, off-target peptides or proteins or fragments thereof comprising said off-target peptides. In some embodiments, the one or more selected antigen-recognition molecules do not detectably bind to any of the tested MHC-off-target peptide complexes, off-target peptides or proteins or fragments thereof comprising said off-target peptides. In some embodiments, the one or more selected antigen-recognition molecules do not detectably bind to any of the tested MHC-off-target peptide complexes, or off-target peptides or proteins or fragments thereof comprising said off-target peptides, when the off-target peptide is present on a surface of a cell at a copy number of at least about 500 to about 10,000 copies / cell. In some embodiments, the one or more selected antigen-recognition molecules do not detectably bind to any of the tested MHC-off-target peptide complexes, or off-target peptides or proteins or fragments thereof comprising said off-target peptides, when the off-target peptide is present on a surface of a cell at a copy number of at least about 500, at least about 600, at least about 700, at least about 800, or at least about 900 copies / cell. In some embodiments, the one or more selected antigen-recognition molecules do not detectably bind to any of the tested MHC-off-target peptide complexes, or off-target peptides or proteins or fragments thereof comprising said off-target peptides, when the off-target peptide is present on a surface of a cell at a copy number of a cell at a copy number of at least about 1,000, at least about 2,000, at least about 3,000, at least about 4,000, at least about 5,000, at least aboutAttorney Docket #: 250298.000961 6,000, at least about 7,000, at least about 8,000, at least about 9,000, or at least about 10,000 copies / cell. In some embodiments, the one or more selected antigen-recognition molecules do not detectably bind to any of the tested MHC-off-target peptide complexes, or off-target peptides or proteins or fragments thereof comprising said off-target peptides, when the off-target peptide is present on a surface of a cell at a copy number of at least about at least about 550 to about 9,800, at least about 600 to about 9,600, at least about 650 to about 9,400, at least about 700 to about 9,200, at least about 750 to about 9,000, at least about 800 to about 8,800, at least about 850 to about 8,600, at least about 900 to about 8,400, at least about 950 to about 8,200, at least about 1000 to about 8,000, at least about 1,050 to about 7,800, at least about 1,100 to about 7,600, at least about 1,150 to about 7,400, at least about 1,200 to about 7,200, at least about 1,250 to about 7,000, at least about 1,300 to about 6,800, at least about 1,350 to about 6,600, at least about 1,400 to about 6,400, at least about 1,450 to about 6,200, or at least about 1,500 to about 6,000 copies / cell. In some embodiments, the one or more selected antigen-recognition molecules do not detectably bind to any of the tested MHC-off-target peptide complexes, or off-target peptides or proteins or fragments thereof comprising said off-target peptides, when the off-target peptide is present on a surface of a cell at a copy number of at least about 1,000 to about 10,000, at least about 1,000 to about 9,500, at least about 1,000 to about 9,000, at least about 1,000 to about 8,500, at least about 1,000 to about 8,000, at least about 1,000 to about 7,500, at least about 1,000 to about 7,000, at least about 1,000 to about 6,500, at least about 1,000 to about 6,000, at least about 1,000 to about 5,500, at least about 1,000 to about 5,000, at least about 1,000 to about 4,500, at least about 1,000 to about 4,000, at least about 1,000 to about 3,500, at least about 1,000 to about 3,000, at least about 1,000 to about 2,500, at least about 1,000 to about 2,000, or at least about 1,000 to about 1,500 copies / cell. In some embodiments, the one or more selected antigen-recognition molecules do not detectably bind to any of the tested MHC-off-target peptide complexes, or off-target peptides or proteins or fragments thereof comprising said off-target peptides, when the off-target peptide is present on a surface of a cell at a copy number of at least about 1,000, at least about 1,010, at least about 1,020, at least about 1,030, at least about 1,040, at least about 1,050, at least about 1,100, at least about 1,150, at least about 1,200, at least about 1,250, at least about 1,300, at least aboutAttorney Docket #: 250298.000961 1,350, at least about 1,400, at least about 1,450, at least about 1,500, at least about 1,550, at least about 1,600, at least about 1,650, at least about 1,700, at least about 1,750, at least about 1,800, at least about 1,850, at least about 1,900, at least about 1,950, or at least about 2,000 copies / cell. In some embodiments, the one or more selected antigen-recognition molecules do not detectably bind to any of the tested MHC-off-target peptide complexes, or off-target peptides or proteins or fragments thereof comprising said off-target peptides, when the off-target peptide is present on a surface of a cell at a copy number of at least about 1,000 copies / cell. In some embodiments, the plurality of antigen-recognition molecules is in a library. The library can be, without limitation, a phage display library or a yeast library. In some embodiments, one or more of the MAGEA3168-176 and / or WT1126-134 peptide, MAGEA3 and / or WT1 protein or fragment thereof comprising said MAGEA3168-176and / or WT1126-134peptide, MHC- MAGEA3168-176and / or MHC-WT1126-134peptide complexes, MHC-off- target peptide complexes, off-target peptides, or proteins or fragments thereof comprising said off- target peptides are immobilized on a solid support. In some embodiments, one or more of the MAGEA3168-176and / or WT1126-134peptide, MAGEA3 and / or WT1 protein or fragment thereof comprising said MAGEA3168-176 and / or WT1126-134 peptide, MHC- MAGEA3168-176 and / or MHC-WT1126-134 peptide complexes, MHC-off- target peptide complexes, off-target peptides, or proteins or fragments thereof comprising said off- target peptides are present on cells (e.g., on the surface of the cells). As a non-limiting example, off-target peptides can be present on cancer cells (e.g., tumor cells), lung cells, liver cells, brain cells, and / or cardiovascular cells. In some embodiments, off-target peptides can be present on cancer cells and / or an antigen-binding molecule targeting MAGEA3168-176 and / or WT1126-134 may be screened for binding and / or reactivity against cancer cells or otherwise immortalized cell lines. In some embodiments, the cancer is a hematologic malignancy, for example, a lymphoma, a leukemia, or a myeloma. In some embodiments, the lymphoma is Hodgkin's lymphoma or non-Hodgkin’s lymphoma. In some embodiments, the leukemia is chronic lymphocytic leukemia (CLL), acute lymphocytic leukemia (ALL), chronic myeloid leukemia (CML), or acute myeloid leukemia (AML). In some embodiments, the cancer is a solid cancer. In one embodiment, the cancer is a head and neck cancer. In one embodiment, the cancer is a renal cell carcinoma. In one embodiment, the cancer is a breast cancer, e.g., triple-negative breast cancer (TNBC). In one embodiment, the cancer is aAttorney Docket #: 250298.000961 non-small cell lung cancer (NSCLC), for example, lung adenocarcinoma. In one embodiment, the cancer is liver hepatocellular carcinoma (HCC). In one embodiment, the cancer is lung squamous cell carcinoma (SCC). In one embodiment, the cancer is bladder cancer. In one embodiment, the cancer is esophageal cancer. In one embodiment, the cancer is uveal melanoma. In one embodiment, the cancer is nasopharyngeal cancer. In one embodiment, the cancer is synovial sarcoma. In one embodiment, the cancer is ovarian cancer. In one embodiment, the cancer is uterine cancer. In one embodiment, the cancer is endometrial cancer. In one embodiment, the cancer is melanoma. In some embodiments, the cancer cell is derived from a tumor cell line (e.g., an endogenous cell line). Non-limiting examples of tumor cell lines include U-87 MG, T98G, NCI- H2023.PRAME-KO, HEP-G2, U-251 MG, NCI-H1915.HLA-A*02:01, OVCAR-3, and NCI- H2023. In some embodiments, the off-target peptides of the present disclosure are present on primary normal cells, which can be derived, e.g., from brain or vasculature, and / or an antigen- binding molecule targeting MAGEA3168-176and / or WT1126-134may be screened for binding and / or reactivity against primary normal cells (e.g., from brain or vasculature). Non-limiting examples of normal cell lines derived from brain include astrocytes (HA-1 cells), brain microvascular endothelial cells (HBMEC-3 cells), and brain vascular pericityes (HBVP-1 cells). Non-limiting examples of normal cell lines derived from vasculature include coronary artery smooth muscle cells (HCASMC-1 cells) and aortic smooth muscle cells (HAoSMC-1 cells). In some embodiments, the off-target peptides of the present disclosure are present on cardiovascular tissue or cells isolated therefrom and / or an antigen-binding molecule targeting MAGEA3168-176and / or WT1126-134may be screened for binding and / or reactivity against cardiovascular tissue or cells isolated therefrom. Such cardiovascular tissue or cells may be derived from, without limitation, coronary artery (with or without plaques), aorta, or ventricle. In some embodiments, the cardiovascular cells can comprise, e.g., cardiomyocytes, endothelial cells, smooth muscle cells, fibroblasts, pericytes, and / or pacemaker cells. In some embodiments, the off-target peptides of the present disclosure are present on cells and / or an antigen-binding molecule targeting MAGEA3168-176and / or WT1126-134may be screened for binding and / or reactivity against cells, which may be part of or sampled from tissues of a subject having a disease, disorder, or condition such as, but not limited to, a cardiovascular disease, disorder, or condition disclosed herein (e.g., myocardial infarction, heart failure, cardiacAttorney Docket #: 250298.000961 insufficiency, coronary insufficiency, pulmonary edema, atherosclerosis, etc.) or a cancer disclosed herein. In some embodiments, the off-target peptides of the present disclosure are present on cells which may be part of or sampled from a diseased tissue of a subject. For example, the cells can be cardiovascular cells which are part of or sampled from a diseased heart tissue such as, but not limited to, diseased ventricle, aorta, and / or coronary artery. In some embodiments, the cells may be part of or sampled from tissues of a subject not having a disease, disorder or condition. In some embodiments, the cells may be part of sampled from a normal tissue of a subject. In various embodiments, the cells are part of or sampled from, for example, without limitation, heart tissue, brain tissue, lung tissue, and / or liver tissue. The heart tissue, brain tissue, lung tissue, and / or liver tissue may be either diseased or normal. In some embodiments, one or more of the MAGEA3168-176and / or WT1126-134, MAGEA3 and / or WT1 protein or fragment thereof comprising said MAGEA3168-176and / or WT1126-134, MHC- MAGEA3168-176 and / or MHC-WT1126-134 peptide complexes, MHC-off-target peptide complexes, off-target peptides, or proteins or fragments thereof comprising said off-target peptides are present in a soluble form. In some embodiments, the level of binding is determined by detecting the amount of antigen-recognition molecules bound to the MAGEA3168-176 and / or WT1126-134 peptide, MAGEA3 and / or WT1 protein or fragment thereof comprising said MAGEA3168-176and / or WT1126-134peptide, MHC- MAGEA3168-176 and / or MHC-WT1126-134 peptide complexes, MHC-off-target peptide complexes, off-target peptides, or proteins or fragments thereof comprising said off-target peptides. In some embodiments of any of the above-described methods, the method is performed in a high-throughput format. In some embodiments, the method is performed in a multi-well plate (e.g., a 96-well plate). Methods to determine binding to pMHC complexes include, for example, surface plasmon resonance (e.g., BIACORETM), or any other biosensor technique, enzyme-linked immunosorbent assay (ELISA), ELISpot, luminescence assay, flow cytometry, chromatography, microscopy, or any suitable immunoassay. Alternatively, or in addition, binding may be determined by functional assays in which a biological response is detected upon binding, for example, cytokine release or cell apoptosis.Attorney Docket #: 250298.000961 For example, antibodies and TCRs may be obtained from display libraries in which a pMHC complex of the disclosure (e.g., a target pMHCs, such as an MHC-MAGEA3168-176and / or MHC-WT1126-134 peptide complex) is used to pan the library. TCRs can be displayed on the surface of phage particles and yeast particles, for example, and such libraries have been used for the isolation of high affinity variants of TCR derived from T cell clones. TCR phage libraries can be used to isolate TCRs with novel antigen specificity. Such libraries can be constructed with α- and β- chain sequences corresponding to those found in a natural repertoire. However, the random combination of these α- and β- chain sequences, which occurs during library creation, can produce a repertoire of TCRs that may not be naturally occurring. In some embodiments, a pMHC complex of the disclosure may be used to screen a library of diverse TCRs displayed on the surface of phage particles. The TCRs displayed by said library may not correspond to those contained in a natural repertoire, for example, they may contain α- and β- chain pairing that would not be present in vivo, and / or the TCRs may contain non-natural mutations and / or the TCRs may be in soluble form. Screening may involve panning the phage library with pMHC complexes of the disclosure and subsequently isolating bound phage particles. For this purpose, pMHC complexes may be attached to a solid support, such as a magnetic bead, or column matrix and phage bound pMHC complexes isolated, with a magnet, or by chromatography, respectively. The panning steps may be repeated several times. Isolated phage may be further expanded in E. coli cells. Isolated phage particles may be tested for specific binding to pMHC complexes of the disclosure. Binding can be detected using techniques described herein such as, but not limited to, ELISA, or SPR for example using a BIACORETMinstrument. The DNA sequence of the T cell receptor displayed by pMHC binding phage can be further identified by PCR methods. Various methods for generating and / or isolating antigen-recognition molecules, such as antibodies and TCRs, including those that target peptides presented as part of pMHC complexes are well known in the art. Antigen-recognition molecules may be generated by immunizing immunocompetent host animals, such as non-human host animals (e.g., rodents such as mice or rats) with antigens such as peptides or pMHC complexes. In certain implementations, the host animal may be genetically modified such that it generates human or humanized antigen recognition molecules in response to the immunization. For instance, TCRs may be generated by immunizing with antigenic peptide (e.g., a target peptide such as MAGEA3168-176and / or WT1126-134) a rodentAttorney Docket #: 250298.000961 genetically modified to express human or humanized TCRs and, optionally, to further express human or humanized MHC (e.g., MHC I α, MHC II α, and / or MHC II β), human or humanized β2 microglobulin (β2M), and / or human or humanized T Cell co receptor (e.g., CD4, CD8 α, and / or CD8 β). See, e.g., U.S. Pat. No. 11,259,510; U.S. Pub. No. 2022 / 0322648; Moore et al., Sci Immunol. 2021 Dec 17; 6(66):eabj4026, which are each herein incorporated by reference in their entirety. Likewise, antibodies, or more specifically TCR-mimetic antibodies, may be generated by immunizing with antigenic pMHC complexes (e.g., a target pMHC complex, such as an MHC- MAGEA3168-176and / or MHC-WT1126-134peptide complex) a rodent genetically modified to express human or humanized immunoglobulins (e.g., IgGs) and, optionally, further express human or humanized MHC (e.g., MHC I α, MHC II α, and / or MHC II β) and / or human or humanized β2 microglobulin (β2M). See, e.g., U.S. Pat No. 8,791,323; U.S. Pat. No. 8,642,835; U.S. Pat. No. 8,754,287; U.S. Pat. No. 10,143,186; U.S. Pat. Pub. No. 2019 / 0292263; Proc Natl Acad Sci U S A. 2014 Apr 8;111(14):5153-8, each of which is herein incorporated by reference in its entirety. Methods of screening antigen-recognition molecules (e.g., cells expressing antigen-recognition molecules such as T cells and B cells) and isolating and cloning sequences, such as variable domain coding sequences, are well known in the art. Alternatively, antigen binding T cells and TCRs can be isolated from fresh blood obtained from patients or healthy donors. Such a method involves stimulating T cells using autologous dendritic cells (DCs), followed by autologous B cells, and then pulsing with a target / off-target peptide disclosed herein. Several rounds of stimulation may be carried out, for example three or four rounds. Activated T cells may then be tested for recognition of the target / off-target peptide by measuring cytokine release in the presence of cells (e.g., T2 cells) loaded with the target / off- target peptide of the disclosure (for example using an IFNγ ELISpot assay). Activated cells may then be sorted by fluorescence-activated cell sorting (FACS) using labelled antibodies to detect intracellular cytokine production (e.g., IFNγ), or expression of a cell surface marker (such as CD137). Sorted cells may be expanded and further validated, for example, by ELISpot assay and / or cytotoxicity against target cells and / or staining by peptide-MHC multimer (e.g., tetramer). The TCR chains from validated clones may then be amplified by rapid amplification of cDNA ends (RACE) and sequenced. Exemplary methods for isolation and validation of TCRs specific to a target antigen are described in Moore et al., Sci. Immunol. 6, eabj4026 (2021); Deering et al.,Attorney Docket #: 250298.000961 Sci Rep. 2023 May 25;13(1):8452; and U.S. Pat. Pub. No. 2021 / 0102942, each of which is herein incorporated by reference in its entirety. Antigen-recognition molecules may be screened for binding to one or more peptides (e.g., target and / or off-target peptides) according to various methods known in the art. The antigen- recognition molecules (e.g., antibodies, TCRs, CARs) and / or the one or more peptides may be presented in solution, presented on a cell surface (e.g., a reporter cell), or immobilized on a solid support, including the specific cells or solid supports described elsewhere herein. For example, the antigen-recognition molecule may be presented on a cell surface (e.g., on a heterologous host cell) or immobilized on a solid support and the one or more peptides may be presented in solution (e.g., as soluble pMHC complexes), presented on a cell surface (e.g., loaded onto MHC of a heterologous cell), or immobilized on a solid support. Similarly, the one or more peptides may be presented on a cell surface (e.g., loaded onto MHC of a heterologous cell) or immobilized on a solid support (e.g., as a pMHC complex) and the antigen-recognition molecule may be presented in solution (e.g., as soluble pMHC complexes), presented on a cell surface (e.g., on a heterologous host cell), or immobilized on a solid support. In some instances, antigen-recognition molecule binding to a peptide presented on a cell surface may be detected using a genetically modified reporter cell that emits a signal in response to the binding, including in cell-to-cell screening systems in which the antigen-recognition molecule and one or more peptides are presented on different cell surfaces. For example, TCR screening can be performed using TCR activation assays. For example, JRT3-T3.5 cells (ATCC TIB-153), a Jurkat subline lacking endogenous TCR surface expression may be utilized as described in Moore et al., Sci. Immunol. 6, eabj4026 (2021), which is herein incorporated by reference in its entirety. T cell receptor alpha (TCRA) and T cell receptor beta (TCRB) sequences of interest can be introduced into the cells by lentiviral transduction, and surface TCR+ cells can be sorted. Antigen-presenting cells (e.g., 293T cells) that are pulsed with a target peptide or off-target peptide can be incubated with the TCR-transduced or parental JRT3 cells. A readout (e.g., luciferase activity) is then measured as an indication of TCR-mediated activation. In some embodiments, monoclonal antibody screening can be performed with cells isolated from the spleens and lymphoid tissue harvested from mice with optimal titers using hybridoma and B cell sorting (BST) platforms. Counter-screening approaches using one or more off-target peptides can help to identify and eliminate B-cells and hybridomas that show cross-Attorney Docket #: 250298.000961 reactivity with peptides that form pHLA complexes resembling the targeted complex. For example, antigen positive (Ag+) clones that have cross-reactivity to off-target peptides can be identified by examining cell supernatants for antibody binding to cells (e.g., T2 cells) pulsed with the target peptide or off-target peptides using a cell binding assay. As another example, Ag+B- cells can be captured using a biotin-labeled HLA-target peptide complex in the presence of high concentrations of one or more unlabeled, HLA-off-target peptide complexes to enrich for antibodies specific for the HLA-target peptide complex. The antibody variable domains of Ag+B- cells can be subsequently cloned as full-length mAbs and expressed (e.g., in CHO cells) for further screening. Antibody binding to target / off-target peptides can be determined using ELISA. For example, MHC-target peptide complexes or MHC-off-target peptide complexes can be coated onto a plate (e.g., 96-well microtiter plate). A sample comprising test antibodies can be added to the plate and the reaction can be incubated under a condition to allow binding to occur. The plate is then washed, and a secondary antibody can be then added to the plate to detect the antibodies bound to an MHC-peptide complex. Typically, the secondary antibody can produce a signal that is indicative of the amount of the antibodies bound to the MHC-peptide complex. In various embodiments of the methods described herein, pMHC complexes may be provided in soluble form, or may be immobilized by attachment to a suitable solid support. Examples of solid supports include, but are not limited to, a bead (e.g., a magnetic bead), a membrane, sepharose, a plate, a tube, a column. pMHC complexes may be attached to an ELISA plate, a magnetic bead, or a surface plasmon resonance biosensor chip. Methods of attaching pMHC complexes to a solid support are known to the skilled person, and include, for example, using an affinity binding pair, e.g., biotin and streptavidin, or antibodies and antigens. In some embodiments, pMHC complexes are labeled with biotin and attached to streptavidin-coated surfaces. In various embodiments of the methods described herein, pMHC complexes may be present on a cell (e.g., on a surface of a cell). Such a cell may be a mammalian cell, preferably a cell of the immune system, and a specialized antigen-presenting cell (APC) such as a dendritic cell or a B cell. Other preferred cells include T2 cells. Cells presenting the peptide or pMHC complex of the disclosure may be isolated, preferably in the form of a homogenous population, or provided in a substantially pure form. Such cells may be obtained by pulsing said cells with one or moreAttorney Docket #: 250298.000961 peptides (e.g., 2 to 10, 2 to 20, 2 to 30, 5 to 25, 5 to 20, or 10 to 15 peptides) of the disclosure, or genetically modifying the cells (via DNA or RNA transfer) to express one or more peptides (e.g., 2 to 10, 2 to 20, 2 to 30, 5 to 25, 5 to 20, or 10 to 15 peptides) of the disclosure. Pulsing involves incubating the cells with the peptide for several hours using peptide concentrations typically ranging from 10−5to 10−12M. Such cells may additionally be transduced with HLA molecules, such as HLA-A*02 (e.g., HLA-A*02:01) or HLA-A*01 (e.g.)HLA-A*01:01 to further induce presentation of the peptide(s). Cells may be produced recombinantly. In various embodiments of the methods described herein, the method is performed in a high-throughput format (e.g., a 96-well plate). In yet another aspect, provided herein is a method of enriching a sample for antigen- recognition molecules that specifically bind a target peptide, comprising (a) contacting a sample comprising a plurality of antigen-recognition molecules with the target peptide in the presence of one or more off-target peptides associated with said target peptide, wherein each of said target peptide and said one or more off-target peptides is presented in a complex with a major histocompatibility complex (MHC) molecule (MHC-target peptide complex or MHC-off-target peptide complex); and (b) enriching the sample by isolating the antigen-recognition molecules that are bound to the MHC-target peptide complex. The method may further comprise repeating steps (a)-(b) to further enrich the sample. In still yet another aspect, provided herein is a method of enriching a sample for antigen- recognition molecules that specifically bind MAGEA3168-176 and / or WT1126-134 peptide, comprising a) contacting a sample comprising a plurality of antigen-recognition molecules with MAGEA3168-176and / or WT1126-134peptide or MAGEA3 and / or WT1 protein or fragment thereof comprising said MAGEA3168-176 and / or WT1126-134 peptide or MAGEA3168-176 and / or WT1126-134 peptide presented in a complex with a major histocompatibility complex (MHC) molecule, or a fragment or derivative thereof (MHC- MAGEA3168-176and / or MHC-WT1126-134peptide complex) in the presence of one or more off-target peptides, wherein each of said off-target peptides (i) comprises an amino acid sequence of any one of SEQ ID Nos: 30-47 and 200-232 and / or 233-240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof, wherein the peptide is 8-12 amino acids in length, wherein each of said one or more off-target peptides is presented in one of the following forms: (1) as a complex with an MHC molecule, or a fragment or derivative thereof (MHC-off-target peptide complex), (2) as a peptide, or (3) as a protein orAttorney Docket #: 250298.000961 fragment thereof comprising said off-target peptide; b) enriching the sample by isolating the antigen-recognition molecules that are detectably bound to said MAGEA3168-176and / or WT1126-134peptide or MAGEA3 and / or WT1 protein or fragment thereof comprising said MAGEA3168-176 and / or WT1126-134peptide or to the MHC- MAGEA3168-176and / or MHC-WT1126-134peptide complex; and c) optionally, repeating steps (a)-(b) using the enriched sample. In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind MAGEA3168-176 peptide, the off-target peptide comprises an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232. In some embodiments of the sample enrichment methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232. In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind MAGEA3168-176peptide, the off-target peptide comprises an amino acid sequence of any one of SEQ ID NOs: 200-232. In some embodiments of the sample enrichment methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 200-232. In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind MAGEA3168-176 peptide, the off-target peptide comprises an amino acid sequence of any one of SEQ ID NOs: 200-201. In some embodiments of the sample enrichment methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 200-201. In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind MAGEA3168-176peptide, the off-target peptide comprises an amino acid sequence of SEQ ID NO: 202-232. In some embodiments of the sample enrichment methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NO: 202-232. In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind MAGEA3168-176peptide, the off-target peptide comprises an amino acid sequence of SEQ ID NO: 202-230. In some embodiments of the sample enrichment methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NO: 202-230.Attorney Docket #: 250298.000961 In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind MAGEA3168-176peptide, the off-target peptide comprises an amino acid sequence of SEQ ID NO: 209, 231, and 232. In some embodiments of the sample enrichment methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NO: 209, 231, and 232. In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind WT1126-134 peptide, the off-target peptide comprises an amino acid sequence of SEQ ID NO: 233-240. In some embodiments of the sample enrichment methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NO: 233- 240. In some embodiments, said MAGEA3168-176and / or WT1126-134peptide or MAGEA3 and / or WT1 protein or fragment thereof comprising said MAGEA3168-176and / or WT1126-134peptide or MHC-MAGEA3168-176 and / or MHC-WT1126-134 peptide complex is present on a cell (e.g., on a surface of a cell) disclosed herein or solid support disclosed herein and said off-target peptides or proteins or fragments thereof comprising said off-target peptides or MHC-off-target peptide complexes are present in solution. In some embodiments, said MAGEA3168-176 and / or WT1126-134 peptide or MAGEA3 and / or WT1 protein or fragment thereof comprising said MAGEA3168-176and / or WT1126-134peptide or MHC- MAGEA3168-176 and / or MHC-WT1126-134 peptide complex is labeled and said off-target peptides or proteins or fragments thereof comprising said off-target peptides or MHC- off-target peptide complexes are not labeled or are labeled differently. In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind MAGEA3168-176 peptide, the MAGEA3168-176 peptide comprises the amino acid sequence EVDPIGHLY (SEQ ID NO: 29) . In some embodiments of the enriching methods, the MAGEA3168-176peptide consists of the amino acid sequence EVDPIGHLY (SEQ ID NO: 29). In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind MAGEA3168-176peptide, the off-target peptide comprises an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232. In some embodiments of the enriching methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232.Attorney Docket #: 250298.000961 In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind MAGEA3168-176peptide, the off-target peptide comprises an amino acid sequence of any one of SEQ ID NOs: 200-232. In some embodiments of the enriching methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 200-232. In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind MAGEA3168-176 peptide, the off-target peptide comprises an amino acid sequence of any one of SEQ ID NOs: 200-201. In some embodiments of the enriching methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 200-201. In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind MAGEA3168-176peptide, the off-target peptide comprises an amino acid sequence of SEQ ID NO: 202-232. In some embodiments of the enriching methods, the off-target peptide consists of an amino acid sequence of SEQ ID NO: 202-232. In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind MAGEA3168-176 peptide, the off-target peptide comprises an amino acid sequence of SEQ ID NO: 202-230. In some embodiments of the enriching methods, the off-target peptide consists of an amino acid sequence of SEQ ID NO: 202-230. In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind MAGEA3168-176 peptide, the off-target peptide comprises an amino acid sequence of SEQ ID NO: 209, 231, and 232. In some embodiments of the enriching methods, the off-target peptide consists of an amino acid sequence of SEQ ID NO: 209, 231, and 232. In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind WT1126-134peptide, the WT1126-134peptide comprises the amino acid sequence RMFPNAPYL (SEQ ID NO: 241). In some embodiments of the enriching methods, the WT1126-134peptide consists of the amino acid sequence EVDPIGHLY(SEQ ID NO: 29) RMFPNAPYL (SEQ ID NO: 241). In some embodiments of the above-described methods of enriching a sample for antigen- recognition molecules that specifically bind WT1126-134 peptide, the off-target peptide comprises an amino acid sequence of any one of SEQ ID NOs: 233-240. In some embodiments of theAttorney Docket #: 250298.000961 enriching methods, the off-target peptide consists of an amino acid sequence of any one of SEQ ID NOs: 233-240. There are various ways that can allow isolation of the antigen-recognition molecules that are bound to the MHC-target peptide complex. For example, the MHC-target peptide complex may be present on antigen-presenting cells while the MHC-off-target peptide complexes are not present on antigen-presenting cells (e.g., in a soluble form). Alternatively, the MHC-target peptide complex may be immobilized on a solid support while the MHC-off-target peptide complexes may be soluble or immobilized to a different solid support. The MHC-target peptide complex and the MHC-off-target peptide complexes may also be differentially labeled such that specific detection and isolation of the MHC-target peptide complex and the antigen-recognition molecules bound thereon can be achieved. The antigen-recognition molecules may be eluted from the MHC-target peptide complex after isolation. Certain embodiments and implementations of the disclosed technology are described above with reference to block and flow diagrams of systems and methods and / or computer program products according to example embodiments or implementations of the disclosed technology. It will be understood that one or more blocks of the block diagrams and flow diagrams, and combinations of blocks in the block diagrams and flow diagrams, respectively, can be implemented by computer-executable program instructions. Likewise, some blocks of the block diagrams and flow diagrams may not necessarily need to be performed in the order presented, may be repeated, or may not necessarily need to be performed at all, according to some embodiments or implementations of the disclosed technology. These computer-executable program instructions may be loaded onto a general-purpose computer, a special-purpose computer, a processor, or other programmable data processing apparatus to produce a particular machine, such that the instructions that execute on the computer, processor, or other programmable data processing apparatus create means for implementing one or more functions specified in the flow diagram block or blocks. These computer program instructions may also be stored in a computer-readable memory that can direct a computer or other programmable data processing apparatus to function in a particular manner, such that the instructions stored in the computer-readable memory produce an article of manufacture including instruction means that implement one or more functions specified in the flow diagram block or blocks.Attorney Docket #: 250298.000961 As an example, embodiments or implementations of the disclosed technology may provide for a computer program product, including a computer-usable medium having a computer- readable program code or program instructions embodied therein, said computer-readable program code adapted to be executed to implement one or more functions specified in the flow diagram block or blocks. Likewise, the computer program instructions may be loaded onto a computer or other programmable data processing apparatus to cause a series of operational elements or steps to be performed on the computer or other programmable apparatus to produce a computer- implemented process such that the instructions that execute on the computer or other programmable apparatus provide elements or steps for implementing the functions specified in the flow diagram block or blocks. Accordingly, blocks of the block diagrams and flow diagrams support combinations of means for performing the specified functions, combinations of elements or steps for performing the specified functions, and program instruction means for performing the specified functions. It will also be understood that each block of the block diagrams and flow diagrams, and combinations of blocks in the block diagrams and flow diagrams, can be implemented by special-purpose, hardware-based computer systems that perform the specified functions, elements or steps, or combinations of special-purpose hardware and computer instructions. Certain implementations of the disclosed technology are described above with reference to customer devices that may include mobile computing devices. Those skilled in the art will recognize that there are several categories of mobile devices, generally known as portable computing devices that can run on batteries but are not usually classified as laptops. For example, mobile devices can include, but are not limited to portable computers, tablet PCs, internet tablets, PDAs, ultra-mobile PCs (UMPCs), wearable devices, and smart phones. Additionally, implementations of the disclosed technology can be utilized with internet of things (IoT) devices, smart televisions and media devices, appliances, automobiles, toys, and voice command devices, along with peripherals that interface with these devices. While certain embodiments of this disclosure have been described in connection with what is presently considered to be the most practical and various embodiments, it is to be understood that this disclosure is not to be limited to the disclosed embodiments, but on the contrary, is intended to cover various modifications and equivalent arrangements included withinAttorney Docket #: 250298.000961 the scope of the appended claims. Although specific terms are employed herein, they are used in a generic and descriptive sense only and not for purposes of limitation. This written description uses examples to disclose certain embodiments of the technology and also to enable any person skilled in the art to practice certain embodiments of this technology, including making and using any apparatuses or systems and performing any incorporated methods. The patentable scope of certain embodiments of the technology is defined in the claims, and may include other examples that occur to those skilled in the art. Such other examples are intended to be within the scope of the claims if they have structural elements that do not differ from the literal language of the claims, or if they include equivalent structural elements with insubstantial differences from the literal language of the claims. Exemplary Compositions In one aspect, the disclosure provides isolated peptides which can be identified, e.g., using any of various methods described herein. In some embodiments, the isolated peptide may be identified for a MAGEA3 and / or WT1 target peptide (e.g., for MAGEA3168-176target EVDPIGHLY (SEQ ID NO: 29) and / or for WT1126-134target RMFPNAPYL (SEQ ID NO: 241)) as described herein. In some embodiments, one or more isolated peptides of the present disclosure comprise an amino acid sequence that is at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90%, at least about 95%, or at least about 99% identical to the amino acid sequence of any one of SEQ ID NOs: 30-47 and 200- 232 and / or 233-240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, one or more isolated peptides of the present disclosure comprise an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232 and / or 233-240. In some embodiments, one or more isolated peptides of the present disclosure consist essentially of an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232 and / or 233-240. In some embodiments, the one or more isolated peptide consist of an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232 and / or 233-240. In some embodiments, the one or more isolated peptides comprise a plurality of isolated peptides. In some embodiments, the one or more isolated peptides comprise two or more sequences selected from any one or SEQ ID NOs: 30-47 and 200- 232 and / or 233-240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof.Attorney Docket #: 250298.000961 In some embodiments, one or more isolated peptides of the present disclosure may have been detected by mass spectrometry as being presented by an HLA molecule in a human tissue sample. In some embodiments, one or more isolated peptides of the present disclosure comprise an amino acid sequence that is at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90%, at least about 95%, or at least about 99% identical to the amino acid sequence of any one of SEQ ID NOs: 30, 31, 32, 39, 41, 43, 44, 45, and 47, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, one or more isolated peptides of the present disclosure comprise an amino acid sequence of any one of SEQ ID NOs: 30, 31, 32, 39, 41, 43, 44, 45, and 47. In some embodiments, one or more isolated peptides of the present disclosure consist essentially of an amino acid sequence of any one of SEQ ID NOs: 30, 31, 32, 39, 41, 43, 44, 45, and 47. In some embodiments, the one or more isolated peptides comprise a plurality of isolated peptides. In some embodiments, the one or more isolated peptides consist of an amino acid sequence of any one of SEQ ID NOs: 30, 31, 32, 39, 41, 43, 44, 45, and 47. In some embodiments, the one or more isolated peptides comprise two or more sequences selected from any one or SEQ ID NOs: 30, 31, 32, 39, 41, 43, 44, 45, and 47, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, one or more isolated peptides of the present disclosure may have been identified through, e.g., a broad bioinformatics screen and / or an X-scan analysis described herein. In some embodiments, one or more isolated peptides of the present disclosure comprise an amino acid sequence that is at least about 60%, at least about 65%, at least about 70%, at least about 75%, at least about 80%, at least about 85%, at least about 90%, at least about 95%, or at least about 99% identical to the amino acid sequence of any one of SEQ ID NOs: 30-47 and 200- 232 and / or 233-240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In some embodiments, one or more isolated peptides of the present disclosure comprise an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232 and / or 233-240. In some embodiments, one or more isolated peptides of the present disclosure consist essentially of an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232 and / or 233-240. In some embodiments, the one or more isolated peptides consist of an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200-232 and / or 233-240. In some embodiments, the one or more isolated peptides comprise a plurality of isolated peptides. In some embodiments, the one or more isolatedAttorney Docket #: 250298.000961 peptides comprise two or more sequences selected from any one or SEQ ID NOs: 30-47 and 200- 232 and / or 233-240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In certain aspects, the present disclosure provides one or more isolated peptides comprising or consisting of an amino acid sequence of any one of SEQ ID NOs: 30-47 and 200- 232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In certain aspects, the present disclosure provides one or more isolated peptides comprising or consisting of an amino acid sequence of any one of SEQ ID NOs: 200-232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In certain aspects, the present disclosure provides one or more isolated peptides comprising or consisting of an amino acid sequence of any one of SEQ ID NOs: 200-201, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In certain aspects, the present disclosure provides one or more isolated peptides comprising or consisting of an amino acid sequence of SEQ ID NOs: 202-232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In certain aspects, the present disclosure provides one or more isolated peptides comprising or consisting of an amino acid sequence of SEQ ID NOs: 202-230, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In certain aspects, the present disclosure provides one or more isolated peptides comprising or consisting of an amino acid sequence of SEQ ID NOs: 209, 231, and 232, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In certain aspects, the present disclosure provides one or more isolated peptides comprising or consisting of an amino acid sequence of SEQ ID NOs: 233-240, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof. In certain aspects, the present disclosure provides one or more isolated peptides comprising or consisting of an amino acid sequence selected from any subset of sequences formed by identifying the common sequences within one or more sets of sequences disclosed herein. In some embodiments, the isolated peptide, or fragment or derivative thereof, is 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, or more, amino acids in length. In some embodiments, the isolated peptides of the disclosure may be about 8-12 amino acids in length. For example, an isolated peptide disclosed herein may be 8 amino acids, 9 amino acids, 10 amino acids, 11 amino acids, or 12 amino acids in length. In some embodiments, the isolated peptides of the disclosure may be about 12-20Attorney Docket #: 250298.000961 amino acids in length. For example, an isolated peptide disclosed herein may be 12 amino acids, 13 amino acids, 14 amino acids, 15 amino acids, 16 amino acids, 17 amino acids, 18 amino acids, 19 amino acids, or 20 amino acids in length. In certain embodiments, the isolated peptide is 8-12 amino acids in length. In certain embodiments, the isolated peptide is 8-11 amino acids in length. In certain embodiments, the isolated peptide is 8-10 amino acids in length. In certain embodiments, the isolated peptide is 9-12 amino acids in length. In certain embodiments, the isolated peptide is 9-11 amino acids in length. In certain embodiments, the isolated peptide is 9-10 amino acids in length. In certain embodiments, the isolated peptide is 9 amino acids in length. Amino acids sequences derived disclosed herein may include naturally occurring proteogenic amino acids as well as non-proteogenic amino acids and non-naturally occurring amino acids such as amino acid analogs. In some embodiments, the amino acids that may be used in the practice of the present disclosure may include, for example, without limitation, naturally occurring proteogenic (L)-amino acids, their optical (D)-isomers, chemically modified amino acids, including, e.g., amino acid analogs such as, e.g., selenocysteine (Sec), penicillamine (3- mercapto-D-valine), pyroglutamic acid (5-oxoproline), etc., naturally occurring non-proteogenic amino acids such as norleucine, and chemically synthesized amino acids that have properties known in the art to be characteristic of an amino acid, and amino acid equivalents. Inserted amino acids and substituted amino acids may be naturally occurring amino acids or may be non-naturally occurring amino acids and, for example, may contain a non-natural side chain, and / or be linked together via non-native peptide bonds. Such altered peptide ligands are discussed further in Douat-Casassus et al., J. Med. Chem, 2007; 50(7):1598-609 and Hoppes et al., J. Immunol 2014; 193(10):4803-13 and references therein. If more than one amino acid residue is substituted and / or inserted, the replacement / inserted amino acid residues may be the same as each other or different from one another. Each replacement amino acid may have a different side chain to the amino acid being replaced. D-amino acids may be substituted for the L-amino acids in the peptides of the disclosure. In addition, non-standard amino acids (i.e., other than the common naturally occurring proteinogenic amino acids such as β-γ-δ-amino acids, as well as many derivatives of L-α-amino acids) may also be used for substitutions or additions to produce peptides of the present disclosure. One can also replace the naturally occurring side chains of the 20 genetically encoded amino acids (or the stereoisomeric D-amino acids) with other side chains, for instance with groupsAttorney Docket #: 250298.000961 such as alkyl, lower alkyl, cyclic 4-, 5-, 6-, to 7-membered alkyl, amide, amide lower alkyl, amide di(lower alkyl), lower alkoxy, hydroxy, carboxy and the lower ester derivatives thereof, and with 4-, 5-, 6-, to 7-membered heterocyclic. For example, proline analogues in which the ring size of the proline residue is changed from 5 members to 4, 6, or 7 members can be employed. Cyclic groups can be saturated or unsaturated, and if unsaturated, can be aromatic or non-aromatic. Heterocyclic groups preferably contain one or more nitrogen, oxygen, and / or sulfur heteroatoms. Examples of such groups include the furazanyl, furyl, imidazolidinyl, imidazolyl, imidazolinyl, isothiazolyl, isoxazolyl, morpholinyl (e.g. morpholino), oxazolyl, piperazinyl (e.g., 1-piperazinyl), piperidyl (e.g., 1-piperidyl, piperidino), pyranyl, pyrazinyl, pyrazolidinyl, pyrazolinyl, pyrazolyl, pyridazinyl, pyridyl, pyrimidinyl, pyrrolidinyl (e.g., 1-pyrrolidinyl), pyrrolinyl, pyrrolyl, thiadiazolyl, thiazolyl, thienyl, thiomorpholinyl (e.g., thiomorpholino), and triazolyl. These heterocyclic groups can be substituted or unsubstituted. Where a group is substituted, the substituent can be alkyl, alkoxy, halogen, oxygen, or substituted or unsubstituted phenyl. Other examples of amino acid replacements include stereoisomers (e.g., D-amino acids) and unnatural amino acids such as, for example, L-ornithine, L-homocysteine, L-homoserine, L- citrulline, 3-sulfino-L-alanine, N-(L-arginino)succinate, 3,4-dihydroxy-L-phenylalanine, 3-iodo- L-tyrosine, 3,5-diiodo-L-tyrosine, triiodothyronine, L-thyroxine, L-selenocysteine, N-(L- arginino)taurine, 4-aminobutylate, (R,S)-3-amino-2-methylpropanoate, a,a-disubstituted amino acids, N-alkyl amino acids, lactic acid, β-alanine, 3-pyridylalanine, 4-hydroxyproline, O- phosphoserine, N-methylglycine, N-acetylserine, N-formylmethionine, 3-methylhistidine, 5- hydroxylysine, nor-leucine, and other similar amino acids and imino acids. In some embodiments, an isolated peptide described herein, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof, can comprise one or more reverse peptide bonds, one or more non-peptide bonds, one or more D-isomers of amino acids, one or more chemical modifications, or any combination thereof. In some embodiments, an isolated peptide described herein, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof, is produced by expression in a heterologous host cell. In some embodiments an isolated peptide described herein, or a pharmaceutically acceptable salt thereof, or a fragment or derivative thereof, is produced synthetically.Attorney Docket #: 250298.000961 In some embodiments, the peptide disclosed herein forms a complex with one or more MHC class I α heavy chains. In some embodiments, the MHC class I α heavy chain is fully human. In some embodiments, the MHC class I α heavy chain is humanized. Humanized MHC class I α heavy chains are described, e.g., in U.S. Pat. Pub. Nos. 2013 / 0111617, 2013 / 0185819 and 2014 / 0245467. In some embodiments, the MHC class I α heavy chain comprises a human extracellular domain (human α1, α2, and / or α3 domains) and a cytoplasmic domain of another species. In some embodiments, the class I α heavy chain polypeptide is HLA-A, HLA-B, HLA- C, HLA-E, HLA-F, HLA-G, HLA-K, or HLA-L. In various aspects, the peptide-MHC can include all the domains of an MHC class I heavy chain. In some embodiments, the MHC molecule is a class I MHC molecule. In some embodiments, the class I MHC molecule is a class I human leukocyte antigen (HLA) molecule. In some embodiments, the class I HLA molecule is HLA-A molecule. In some embodiments, the HLA-A molecule is an HLA-A2 molecule. In some specific embodiments, the HLA-A2 molecule is HLA-A*02:01 molecule. In some embodiments, the MHC molecule comprises a β2-microglobulin. In some embodiments, the β2-microglobulin is fully human. In some embodiments, the β2-microglobulin is humanized. In some embodiments, the MHC class I molecule comprises a mutation in a β2- microglobulin (β2m or Β2M) polypeptide and in the Heavy Chain sequence to affect a disulfide bond between the Β2M and the Heavy Chain. In some cases, the Heavy Chain is an HLA and wherein the disulfide bond links one of the following pairs of residues: Β2M residue 12, HLA residue 236; Β2M residue 12, HLA residue 237; Β2M residue 8, HLA residue 234; Β2M residue 10, HLA residue 235; Β2M residue 24, HLA residue 236; Β2M residue 28, HLA residue 232; Β2M residue 98, HLA residue 192; Β2M residue 99, HLA residue 234; Β2M residue 3, HLA residue 120; Β2M residue 31, HLA residue 96; Β2M residue 53, HLA residue 35; Β2M residue 60, HLA residue 96; Β2M residue 60, HLA residue 122; Β2M residue 63, HLA residue 27; Β2M residue Arg3, HLA residue Gly120; Β2M residue His31, HLA residue Gln96; Β2M residue Asp53, HLA residue Arg35; Β2M residue Trp60, HLA residue Gln96; Β2M residue Trp60, HLA residue Asp122; Β2M residue Tyr63, HLA residue Tyr27; Β2M residue Lys6, HLA residue Glu232; Β2M residue Gln8, HLA residue Arg234; Β2M residue Tyr10, HLA residue Pro235; Β2M residue Ser11, HLA residue Gln242; Β2M residue Asn24, HLA residue Ala236; Β2M residue Ser28, HLA residue Glu232; Β2M residue Asp98, HLA residue His192; and Β2M residue Met99, HLA residueAttorney Docket #: 250298.000961 Arg234, first linker position Gly2, Heavy Chain (HLA) position Tyr84; Light Chain (Β2M) position Arg12, HLA Ala236; and / or Β2M residue Arg12, HLA residue Gly237. In some embodiments, at least one chain of the MHC and the peptide are comprised within a fusion protein. In one specific embodiment, the MHC and the peptide are separated by a linker sequence. For example, the single chain molecule can comprise, from amino to carboxy terminal, an antigenic determinant, a β2-microglobulin sequence, and a class I α (heavy) chain sequence. Alternatively, the single chain molecule can comprise, from amino to carboxy terminal, an antigenic determinant, a class I α (heavy) chain sequence, and a β2-microglobulin sequence. The single-chain molecule can further comprise a signal peptide sequence at the amino terminal. In certain embodiments, there can be a linker sequence between the peptide sequence and the β2- microglobulin sequence. In certain embodiments, there can be a linker sequence between the β2- microglobulin sequence and the class I α (heavy) chain sequence. A single-chain molecule can further comprise a signal peptide sequence at the amino terminal, as well as first linker sequence extending between the peptide sequence and the β2-microglobulin sequence, and / or a second linker sequence extending between the β2-microglobulin sequence and the class I heavy chain sequence. In certain embodiments, the β2-microglobulin and the class I α (heavy) chain sequences can be human, murine, or porcine. In some embodiments, a single-chain molecule can comprise a first flexible linker between the peptide ligand segment and the β2-microglobulin segment. For example, linkers can extend from and connect the carboxy terminal of the peptide ligand segment to the amino terminal of the β2-microglobulin segment. Preferably, the linkers are structured to allow the linked peptide ligand to fold into the binding groove resulting in a functional MHC-antigen peptide. In some embodiments, this linker can comprise at least about 10 amino acids, up to about 15 amino acids. In some embodiments, a single-chain molecule can comprise a second flexible linker inserted between the β2-microglobulin and heavy chain segments. For example, linkers can extend from and connect the carboxy terminal of the β2-microglobulin segment to the amino terminal of the heavy chain segment. In certain embodiments, the β2-microglobulin and the heavy chain can fold into the binding groove resulting in a molecule which can function in promoting T cell expansion. Suitable linkers used in the MHCs can be of any of a number of suitable lengths, such as from 1 amino acid (e.g., Gly) to 20 amino acids, from 2 amino acids to 15 amino acids, from 3 amino acids to 12 amino acids, including 4 amino acids to 10 amino acids, 5 amino acids to 9Attorney Docket #: 250298.000961 amino acids, 6 amino acids to 8 amino acids, or 7 amino acids to 8 amino acids, and can be 1, 2, 3, 4, 5, 6, or 7 amino acids. Non-limiting examples of linkers include, e.g., glycine polymers (G)n, glycine-serine polymers (including, for example, (GS)n, (GSGGS)n (SEQ ID NO: 147) and (GGGS)n (SEQ ID NO: 148), where n is an integer of at least one), glycine-alanine polymers, alanine-serine polymers, and other flexible linkers. Glycine and glycine-serine polymers can be used; both Gly and Ser are relatively unstructured, and therefore can serve as a neutral tether between components. Glycine polymers can be used; glycine accesses significantly more phi-psi space than even alanine, and is much less restricted than residues with longer side chains). Exemplary linkers can comprise amino acid sequences including, but not limited to, those listed in Table 1. In some embodiments, a linker peptide includes a cysteine residue that can form a disulfide bond with a cysteine residue present in a second polypeptide. Table 1. Examples of Linker Sequences Linker amino acid SEQ Linker codon-optimized SEQ Linker codon-optimized SEQ sequence ID nucleotide sequence ID nucleotide sequence ID :Attorney Docket #: 250298.000961 GGGASGGGGSGG 110 GGGGGGGGCGCTTCA 126 GGAGGCGGCGCTTCTG 142 GGS GGCGGAGGTGGAAGT GGGGCGGGGGTAGTGlently attached to an MHC class I α (heavy) chain via a disulfide bridge (i.e., a disulfide bond between two cystines). In certain embodiments, the disulfide bond comprises a first cysteine, comprising a linker extending from the carboxy terminal of an antigen peptide, and a second cysteine comprising an MHC class I heavy chain (e.g., an MHC class I α (heavy) chain which has a non- covalent binding site for the antigen peptide). In certain embodiments, the second cysteine can be a mutation (addition or substitution) in the MHC class I α (heavy) chain. In certain embodiments, the single-chain molecule can comprise one contiguous polypeptide chain as well as a disulfide bridge. In certain embodiments, the single-chain molecule can comprise two contiguous polypeptide chains which are attached via the disulfide bridge as the only covalent linkage. In some embodiments, the linking sequences can comprise at least one amino acid in addition to the Cys residues, including one or more Gly residues, one or more Ala residues, and / or one or more Ser residues. In certain embodiments, the disulfide bridge can link an antigen peptide described herein in the class I groove of the pMHC complex if the pMHC complex comprises a first cysteine in a Gly-Ser linker extending between the C-terminus of the peptide and the β2-microglobulin, and a second cysteine in a proximal heavy chain position.Attorney Docket #: 250298.000961 Attaching the peptide to the MHC class I or MHC class II molecule via a flexible linker has the can help ensure that the peptide will occupy and stay associated with the MHC molecule during biosynthesis, transport, and display. However, there may be situations in which this linker can interfere with peptide binding to the MHC molecule or with recognition of the complex by an antigen-recognition molecule. As an alternate approach, in some embodiments, the MHC molecule and the peptide are expressed separately. In some embodiments, the β2-microglobulin sequence can comprise a full-length β2- microglobulin sequence. In certain embodiments, the β2-microglobulin sequence lacks the leader peptide sequence. As such, in some configurations, the β2-microglobulin sequence can comprise about 99 amino acids, and can be a mouse β2-microglobulin sequence (e.g., GenBank Accession No. X01838). In some other configurations, the β2-microglobulin sequence can comprise about 99 amino acids, and can be a human β2-microglobulin sequence (e.g., GenBank Accession No. AF072097.1). In some embodiments, a peptide of the present disclosure may be covalently linked to an MHC molecule, such as by a disulfide bond. In some embodiments, the pMHC complex can contain MHC sequences as disclosed in U.S. Patent Nos. 4,478,823; 6,011,146; 8,518,697; 8,895,020; 8,992,937; WO 96 / 04314; Mottez et al. J. Exp. Med. 181: 493-502, 1995; Madden et al. Cell 70: 1035-1048, 1992; Matsumura et al., Science 257: 927-934, 1992; Mage et al., Proc. Natl. Acad. Sci. USA 89: 10658-10662, 1992; Toshitani et al., Proc. Nat’l Acad. Sci.93: 236-240, 1996; Chung et al, J. Immunol. 163:3699-3708, 1999; Uger and Barber, J. Immunol. 160: 1598- 1605, 1998; Uger et al., J. Immunol. 162, pp. 6024-6028, 1999; White et al., J. Immunol. 162: 2671-2676, 1999; Yu et al., J. Immunol. 168:3145-3149, 2002; Truscott et al., J. Immunol. 178: 6280–6289, 2007; Mitaksov et al., Chem Biol.2007 August; 14(8):909–922; Hansen et al., Trends Immunol. 2010 Oct; 31(10):363-9, all of which are incorporated by reference in their entireties. In some embodiments, the MHC comprises a class II MHC polypeptide or a fragment, mutant or derivative thereof. In one specific embodiment, the MHC comprises α and β polypeptides of a class II MHC complex or a fragment, mutant or derivative thereof. In one specific embodiment, the α and β polypeptides are linked by a peptide linker. In one specific embodiment, the MHC comprises α and β polypeptides of a human class II MHC complex selected from the group consisting of HLA-DP, HLA-DR, HLA-DQ, HLA-DM and HLA-DO. In anotherAttorney Docket #: 250298.000961 specific embodiment, the MHC comprises α and β polypeptides of a murine H-2A or H-2E class II MHC complex. Naturally occurring MHC class II molecules can contain two polypeptide chains, α and β. The chains may come from the DP, DQ, or DR gene groups. There are about 40 known different human MHC class II molecules. All have the same basic structure but can vary subtly in their molecular structure. MHC class II molecules can bind peptides of 13-18 amino acids in length. In some embodiments, the MHC class II α chain is fully human. In some embodiments, the MHC class II α chain is humanized. Humanized MHC class II α chains are described, e.g., in U.S. Pat. Nos. 8,847,005, 9,043,996, and 10,154,658, which are incorporated herein by reference in their entireties. In some embodiments, the humanized MHC class II α chain polypeptide comprises a human extracellular domain and a cytoplasmic domain of another species. In some embodiments, the class II α chain is HLA-DMA, HLA-DOA, HLA-DPA, HLA-DQA or HLA- DRA. In some embodiments, the class II α chain polypeptide is humanized HLA-DMA, HLA- DOA, HLA-DPA, HLA-DQA and / or HLA-DRA. In some embodiments, the peptide of the present disclosure forms a complex with one or more MHC class II β chains. In some embodiments, the MHC class II β chain is fully human. In some embodiments, the MHC class II β chain polypeptide is humanized. Humanized MHC class II β chain polypeptides are described, e.g., in U.S. Pat. Nos.8,847,005, 9,043,996, and 10,154,658, which are incorporated herein by reference in their entireties. In some embodiments, the humanized MHC class II β chain comprises a human extracellular domain and a cyto...

Claims

1. Attorney Docket #: 250298.000961 CLAIMS What is claimed is:

1. A method for providing one or more off-target 3D computational models of a potential off- target peptide in a groove of an MHC molecule (“comparison MHC-off-target models”) for comparison to a 3D computational model of a target peptide in a complex with the MHC molecule (“MHC-target model”), the method comprising: generating a coarse-grained model of the potential off-target peptide in the groove of the MHC molecule (“coarse-grained MHC-off-target model”) by a substituting, in the MHC-target model, an amino acid sequence of the potential off-target peptide in place of an amino acid sequence of the target peptide; generating a plurality of refined computational models of the potential off-target peptide in the groove of the MHC molecule (“refined MHC-off-target models”) by computationally optimizing the coarse-grained MHC-off-target model multiple times such that each optimization of the coarse-grained MHC-off-target model results in a respective refined MHC-off-target model of the plurality of refined MHC-off-target models; and selecting the one or more comparison MHC-off-target models from the plurality of refined MHC-off-target models such that the one or more comparison MHC-off-target models have lower energy than a majority of the plurality of the refined MHC-off-target models.

2. The method of claim 1, further comprising: selecting a 3D computational model of a template peptide bound to the MHC molecule (“MHC-template model”) from a database of known protein structures based at least in part on amino acid sequence similarity of the template peptide to the target peptide; and generating the MHC-target model based at least in part on the MHC-template model.

3. The method of claim 1, further comprising: generating the MHC-target model based at least in part on an experimentally determined 3D structure of the target peptide in a complex with the MHC molecule.Attorney Docket #: 250298.000961 4. The method of any one of claims 1-3, wherein generating the coarse-grained MHC-off- target model comprises optimizing a selection of rotamer combinations for the off-target peptide and MHC molecule to eliminate steric clashes.

5. The method of any one of claims 1-4, wherein generating the plurality of refined MHC- off-target models comprises executing computational peptide docking algorithm on the coarse- grained MHC-off-target model.

6. The method of claim 5, wherein the computational peptide docking algorithm comprises a Monte Carlo search with minimization algorithm.

7. The method of claim 6, wherein the minimization algorithm is applied to a backbone of the off-target peptide, and wherein peptide docking algorithm comprises on-the-fly side-chain optimization of the off- target peptide.

8. The method of any one of claims 5-7, wherein the computational peptide docking algorithm comprises the following steps: a) modifying an energy function used to evaluate an MHC-peptide model by reducing the weight of van der Waals repulsive forces and / or increasing the weight of van der Waals attractive forces, optionally both, to an extent that will permit sampling of alternative conformations of the MHC-peptide model while preventing a peptide of the MHC-peptide model from separating from a binding pocket within the groove of the MHC molecule during a subsequent energy minimization reconfiguration of the MHC-peptide model; b) optimizing a rigid body orientation of the peptide of the MHC-peptide model by applying a random rigid body perturbation, optionally a Gaussian rigid body perturbation, comprising a rotation and / or translation to affect the orientation of the peptide within the MHC- peptide model with respect to the groove, repacking the side chains of rotamers within a peptide- MHC interface of the MHC-peptide model following the random rigid body perturbation, and applying an energy minimization step following the repacking to arrive at a reconfigured rigid body orientation, wherein the repacking comprises optimizing the selection of rotamerAttorney Docket #: 250298.000961 combinations for the peptide-MHC interface to eliminate steric clashes, wherein the energy minimization step comprises using a deterministic algorithm to find a local energy minimum, wherein the reconfigured rigid body orientation is accepted only if an energy function criterion, optionally the Metropolis criterion, is met, and wherein the applying of the random rigid body perturbation, the repacking, and the energy minimization step are sequentially repeated for a plurality of cycles, optionally a predefined number of cycles and / or until an energy criterion is satisfied; c) optimizing the peptide backbone conformation, following optimization of the rigid body orientation, by applying a random torsion angle perturbation to the peptide backbone, optionally comprising a Rosetta small move or a Rosetta shear move, repacking the side chains of rotamers within the peptide-MHC interface following the random torsion angle perturbation, and applying an energy minimization step following the repacking to arrive at a reconfigured peptide backbone conformation, wherein the repacking comprises optimizing the selection of rotamer combinations for the peptide-MHC interface to eliminate steric clashes, wherein the energy minimization step comprises using a deterministic algorithm to find a local energy minimum, wherein the reconfigured peptide backbone conformation is accepted only if an energy function criterion, optionally the Metropolis criterion, is met, and wherein the applying of the random torsion angle perturbation, the repacking, and the energy minimization step are sequentially repeated for a plurality of cycles, optionally a predefined number of cycles and / or until an energy criterion is satisfied, optionally wherein the random torsion angle perturbation alternates between Rosetta small moves and Rosetta shear moves each cycle; and d) repeating steps (b) and (c) for a plurality of cycles wherein the van der Waals forces are gradually ramped back towards normal values such that the last cycle is performed with the normal values to arrive at a refined MHC-off-target model of the plurality of refined MHC-off-target models.

9. The method of any one of claims 5-8, further comprising: repeating the computational peptide docking algorithm a plurality of times, optionally at least 100, 200, 500, 1,000, 2,000, 5,000, or 10,000 times, to produce the plurality of refined MHC- off-target models.Attorney Docket #: 250298.000961 10. The method of any one of claims 1-9, wherein generating a plurality of refined computational models comprises generating at least 100, 200, 500, 1,000, 2,000, 5,000, or 10,000 refined MHC-off-target models based at least in part on the coarse-grained MHC-off-target model.

11. The method of any one of claims 1-10, wherein the one or more comparison MHC-off- target peptide models consist of a predetermined number, optionally at least 5, of the refined MHC- off-target models having the lowest energy scores as evaluated by an energy function.

12. The method of claim 11, further comprising: calculating, for each of the plurality of refined three-dimensional models, a total energy score of an MHC-peptide complex, an interface score that measures an energy of pairwise interactions across a peptide-MHC interface, a peptide score that measures an energy function over the residues of the peptide, or a combination thereof, optionally a weighted sum.

13. The method of any one of claims 1-12, wherein the one or more comparison MHC-off- target peptide models consist of a predetermined number, optionally at least 5, of the refined MHC- off-target models having a higher stability than a majority of the refined MHC-off-target models.

14. A method for quantifying structural similarity between a potential off-target peptide in a groove of an MHC molecule and a target peptide in complex with the MHC molecule for the purposes of antigen-recognition molecule binding, the method comprising: obtaining a plurality of 3D computational models of the potential off-target peptide in the groove of the MHC molecule (“comparison MHC-off-target models”); calculating, for each of the plurality of comparison MHC-off-target models, one or more structural similarity metrics such that each of the one or more structural similarity metrics comprises a corresponding value for each of the plurality of comparison MHC-off-target models and represents a measure of structural similarity between the comparison MHC-off-target model and a 3D computational model of the target peptide in complex with the MHC molecule (“MHC- target model”); and calculating, for each of the one or more structural similarity metrics, a single composite structural similarity metric comprising a value based at least in part on the corresponding structuralAttorney Docket #: 250298.000961 similarity metric values for at least a portion of the plurality of comparison MHC-off-target models.

15. The method of claim 14, wherein obtaining the one or more comparison MHC-off-target models comprises providing one or more, optionally all, of the plurality of comparison MHC-off- target models according to any one of claims 1-12.

16. The method of claim 14 or 15, further comprising: obtaining the MHC-target model and / or one or more of the plurality of comparison MHC- off-target models, at least in part, from a predicted structure determined using one or more of the following: a) template-based modeling; b) sequence-based machine learning; and / or c) experimental measurements, optionally wherein the experimental measurements are made using X-ray crystallography or Cryo-electron microscopy (Cryo-EM).

17. The method of claim 16, further comprising: obtaining the MHC-target model and / or at least a portion of the plurality of comparison MHC-off-target models by a template-based modeling process comprising: a) searching a database of known protein structures comprising a template peptide bound to the MHC molecule to identify a plurality of template structures based, at least in part, on amino acid sequence similarity of the template peptide with the peptide sequence of the target peptide or potential off-target peptide; b) aligning the peptide sequence to each of the three-dimensional structures of the template structures based on a comparison of the sequences; c) calculating an energy score for each of the aligned peptide sequences; d) selecting a template structure based on the calculated energy scores; and e) assigning a predicted structure based on the selected template structure.Attorney Docket #: 250298.000961 18. The method of claim 16 or 17, further comprising: determining the predicted structure(s) using a sequence-based machine learning algorithm, optionally wherein the sequence-based machine learning algorithm uses a neural network-based model.

19. The method of any one of claims 14-18, further comprising: determining the MHC-target model and / or at least a portion of the plurality of comparison MHC-off-target models, at least in part, from a prepacked predicted structure, wherein the prepacked predicted structure is optimized based at least in part on the selection of rotamer combinations for the peptide and MHC molecule to eliminate steric clashes, optionally wherein the predicted structure is based at least in part on a templated-based modeling or experimental measurements followed by prepacking.

20. The method of any one of claims 14-19, further comprising: determining the MHC-target model and the plurality of comparison MHC-off-target models, at least in part, from predicted structures determined using the same approach, optionally template-based modeling or sequence-based machine learning.

21. The method of any one of claims 14-20, further comprising: generating the MHC-target model by refining an initial coarse-grained MHC-target model by a computational peptide docking algorithm, optionally wherein the initial coarse-grained MHC- target model is a predicted structure of any one of claims 23-27, optionally wherein the predicted structure is a prepacked predicted structure.

22. The method of any one of claims 14-21, generating at least a portion of the plurality of comparison MHC-off-target models by refining a coarse-grained MHC-off-target model by a computational peptide docking algorithm, optionally wherein the coarse-grained MHC-off-target model is a predicted structure of any one of claims 23-27, optionally wherein the predicted structure is a prepacked predicted structure.Attorney Docket #: 250298.000961 23. The method of claim 21 or 22, wherein the computational peptide docking algorithm comprises a Monte Carlo search with minimization algorithm.

24. The method of any one of claims 21-23, wherein the computational peptide docking algorithm comprises the following steps: a) modifying an energy function used to evaluate an MHC-peptide model by reducing the weight of van der Waals repulsive forces and / or increasing the weight of van der Waals attractive forces, optionally both, to an extent that will permit sampling of alternative conformations of the MHC-peptide model while preventing a peptide of the MHC-peptide model from separating from a binding pocket within the groove of the MHC molecule during a subsequent energy minimization reconfiguration of the MHC-peptide model; b) optimizing a rigid body orientation of the peptide of the MHC-peptide model by applying a random rigid body perturbation, optionally a Gaussian rigid body perturbation, comprising a rotation and / or translation to affect the orientation of the peptide within the MHC- peptide model with respect to the groove, repacking the side chains of rotamers within a peptide- MHC interface of the MHC-peptide model following the random rigid body perturbation, and applying an energy minimization step following the repacking to arrive at a reconfigured rigid body orientation, wherein the repacking comprises optimizing the selection of rotamer combinations for the peptide-MHC interface to eliminate steric clashes, wherein the energy minimization step comprises using a deterministic algorithm to find a local energy minimum, wherein the reconfigured rigid body orientation is accepted only if an energy function criterion, optionally the Metropolis criterion, is met, and wherein the applying of the random rigid body perturbation, the repacking, and the energy minimization step are sequentially repeated for a plurality of cycles, optionally a predefined number of cycles and / or until an energy criterion is satisfied; c) optimizing the peptide backbone conformation, following optimization of the rigid body orientation, by applying a random torsion angle perturbation to the peptide backbone, optionally comprising a Rosetta small move or a Rosetta shear move , repacking the side chains of rotamers within the peptide-MHC interface following the random torsion angle perturbation, and applying an energy minimization step following the repacking to arrive at a reconfigured peptide backbone conformation, wherein the repacking comprises optimizing the selection of rotamer combinationsAttorney Docket #: 250298.000961 for the peptide-MHC interface to eliminate steric clashes, wherein the energy minimization step comprises using a deterministic algorithm to find a local energy minimum, wherein the reconfigured peptide backbone conformation is accepted only if an energy function criterion, optionally the Metropolis criterion, is met, and wherein the applying of the random torsion angle perturbation, the repacking, and the energy minimization step are sequentially repeated for a plurality of cycles, optionally a predefined number of cycles and / or until an energy criterion is satisfied, optionally wherein the random torsion angle perturbation alternates between Rosetta small moves and Rosetta shear moves each cycle; and d) repeating steps (b) and (c) for a plurality of cycles wherein the van der Waals forces are gradually ramped back towards normal values such that the last cycle is performed with the normal values to arrive at a refined MHC-off-target model of the plurality of refined MHC-off-target models.

25. The method of any one of claims 21-24, further comprising: repeating the computational peptide docking algorithm a plurality of times, optionally at least 100, 200, 500, 1,000, 2,000, 5,000, or 10,000 times, to produce a plurality of refined MHC- off-target models, wherein the plurality of comparison MHC-off-target models comprises a portion of the refined MHC-off-target models having lower energy than a majority of the plurality of refined MHC-off-target models.

26. The method of any one of claims 14-25, wherein the one or more structural similarity metrics comprises a difference value which quantifies distances between atoms of the MHC-target model and corresponding atoms of a respective comparison MHC-off-target model of the plurality of comparison MHC-off-target models, optionally wherein the difference value is based on an average distance such as root mean square deviations (RMSDs).

27. The method of claim 26, wherein the difference value quantifies distances between heavy atoms only.Attorney Docket #: 250298.000961 28. The method of claim 26 or 27, wherein the distances comprise the distances between all heavy atoms of the target peptide backbone and all corresponding heavy atoms of each of the potential off-target peptide backbones.

29. The method of claim 27 or 28, wherein the distances consist of the distances between atoms, optionally all heavy atoms, of the target peptide backbone of the MHC-target model at each position that has been determined to be available for binding by an antigen-recognizing molecule to a peptide-MHC (pMHC) complex comprising the target peptide bound to the MHC molecule and all corresponding atoms of the potential off-target peptide backbones of the plurality of comparison MHC-off-target models at each of the corresponding positions, optionally wherein the positions available for binding an antigen-recognizing molecule have been predicted by a mutagenesis screen to be those positions that, based on changes in binding affinity, are not involved in binding the MHC molecule, and optionally wherein the mutagenesis screen is a computational mutagenesis screen and those positions that are not involved in binding the MHC molecule are determined by a machine learning model, such as an artificial neural network, trained on peptide-MHC binding data.

30. The method of claim 28, wherein the distances consist of the distances between all heavy atoms of the target peptide backbone of the MHC-target model and all corresponding heavy atoms of each of the potential off-target peptide backbones of the plurality of comparison MHC-off-target models.

31. The method of claim 28, wherein the distances comprise the distances between heavy atoms of at least a portion of the groove of the MHC molecule in the MHC-target model and a corresponding portion of the groove of the MHC molecule in each of the plurality of comparison MHC-off target models, optionally wherein the portion comprises the bed and rails of the groove.

32. The method of claim 31, wherein the portion consists of the bed and the rails of the groove.Attorney Docket #: 250298.000961 33. The method of any one of claims 14-32, wherein the one or more structural similarity metrics comprises a quantification of a correlation (“correlation quantification”) between a molecular surface interaction fingerprint of the MHC-target model and each of the plurality of comparison MHC-off-target models, wherein the molecular surface interaction fingerprint characterizes an interaction probability of a respective model with an antigen-binding molecule based on one or more surface features, wherein the one or more surface features comprise geometric features and / or chemical features of the molecular surface, optionally wherein the molecular surface interaction fingerprint is a vector, optionally wherein the correlation quantification comprises a correlation coefficient such as a Pearson correlation coefficient, and optionally wherein the geometric features comprise shape index or distance-dependent curvature and / or the chemical features comprise hydropathy, continuum electrostatics, or location of free electrons and proton donors.

34. The method of claim 33, wherein the molecular surface interaction fingerprint is a vector of interaction scores, wherein each interaction score is associated with a spatially localized portion of the molecular surface of the respective model and is a scalar value representative of a probability of the respective spatially localized portion being involved in a protein-protein interaction, optionally wherein each spatially localized portion is one of a plurality of overlapping patches that encompass the entire molecular surface of the respective model, further optionally wherein the vector comprises an interaction score for each patch of the plurality of patches.

35. The method of claim 34, wherein each patch of the plurality of overlapping patches is a geodesic patch having a fixed geodesic distance from a patch center, optionally wherein the patch center is a vertex of the molecular surface of the respective model and optionally wherein each patch has the same fixed geodesic distance.

36. The method of any one of claims 33-35, wherein the molecular surface interaction fingerprint is determined at least in part by geometric deep learning, optionally using a convolutional neural network.Attorney Docket #: 250298.000961 37. The method of any one of claims 33-36, wherein the molecular surface interaction fingerprint is determined by: a) decomposing a surface of the respective model into a plurality of overlapping geodesic patches; b) mapping the one or more surface features of the respective model to each of the geodesic patches using polar geodesic coordinates, wherein the one or more surface features comprise one or more, optionally all, of the following features: shape index, distance-dependent curvature, hydropathy, continuum electrostatics, and location of free electrons and proton donors; c) applying a convolutional neural network to each patch to produce an interaction score for each patch, wherein applying the convolutional neural network comprises rotating the geodesic patch to provide rotation invariance, and wherein the convolutional neural network has been trained on i) portions of surfaces that form interface regions between pairs of proteins that are known binding partners and ii) portions of surfaces that do not form interface regions between pairs of proteins, optionally wherein the interface regions are solvent inaccessible regions in complexes of the known binding partners and optionally wherein the proportions of surfaces that do not form interface regions are derived from one or both of the known binding partners; and d) determining the molecular surface interaction fingerprint based at least in part on the interaction scores of the plurality of overlapping geodesic patches, wherein determining the molecular surface interaction fingerprint comprises identifying spatially corresponding patches between the MHC-target model and each respective MHC off-target model and wherein the molecular surface interaction fingerprint comprises the interaction scores for the corresponding patches, optionally wherein determining the molecular surface interaction fingerprint comprises removing interaction scores that are not associated with a corresponding patch.

38. The method of claim 37, wherein mapping the surface features to the geodesic patches comprises locally averaging the one or more surface features to learnable Gaussian kernels.

39. The method of any one of claims 14-38, wherein the plurality of comparison MHC-off- target models comprises a predetermined number of models, optionally, at least 5.Attorney Docket #: 250298.000961 40. The method of any one of claims 14-39, wherein the composite structural similarity metric of each of the one or more structural similarity metrics is based at least in part on an aggregate measure of a respective structural similar metric for each of the plurality of comparison MHC-off- target models.

41. The method of claim 40, wherein the aggregate measure comprises an average, median, or minimum.

42. The method of claim 39, wherein the aggregate measure comprises a median of the respective structural similar metric for each of the plurality of comparison MHC-off-target models.

43. The method of any one of claims 14-42, wherein the one or more structural similarity metrics comprises at least one of: a first RMSD metric based on similarity of an overall peptide-MHC complex structure that includes only the peptide and the binding groove region of the MHC molecule; a second RMSD metric based on similarity of peptide conformation in the MHC groove; a third RMSD metric based on similarity of conformation of peptide residue positions available for antigen-recognition molecule binding; or a fourth metric based on correlation between computed interaction scores associated with portions of a peptide-MHC molecular surface that comprises protein surfaces important for biomolecular interaction.

44. A method for identifying potential off-target peptide(s) based on sequence similarity and structural similarity for an antigen-recognition molecule that recognizes a target peptide presented in complex with an MHC molecule (MHC-target peptide complex), the method comprising: obtaining a pool of peptides of suitable length, optionally wherein the pool of peptides are expressed in normal tissues, optionally essential, normal tissues; identifying, within the pool, high sequence similarity peptides that have (i) more amino acid sequence similarity to the target peptide than a majority of peptides within the pool and (ii) have a binding affinity to the MHC molecule greater than a threshold value; andAttorney Docket #: 250298.000961 identifying the potential off-target peptides by selecting within the high sequence similarity peptides, the peptide(s) that are more structurally similar, when positioned in a groove of the MHC molecule, to the MHC-target peptide complex than a majority of the high sequence similarity peptides.

45. The method of claim 44, wherein identifying, within the high sequence similarity peptides, the high sequence similarity and structurally similar off-target peptide(s) comprises: quantifying structural similarity between each of the high sequence similarity peptides in a groove of the MHC molecule and the target peptide in the groove of the MHC molecule for the purposes of antigen-recognition molecule binding according to the method of any one of claims 21-43, wherein each of the high sequence similarity peptides is the potential off-target peptide of claims 21-43.

46. The method of claim 44 or 45, wherein identifying, within the pool, high sequence similarity peptides comprises identifying peptides within the pool based on one or more of the following: a) a degree of similarity between a sequence of a peptide within the pool and a target peptide sequence of the target peptide, optionally wherein a threshold degree of similarity for selection requires one or more residue mismatches and / or requires one or more identical residues; b) a number of identical residues, optionally at least three, at positions within the target peptide sequence that have been determined to be available for binding by an antigen-recognizing molecule to a peptide-MHC (pMHC) complex comprising the target peptide bound to the MHC molecule, optionally wherein the positions available for binding an antigen-recognizing molecule have been predicted by a mutagenesis screen to be those positions that, based on changes in binding affinity, are not involved in binding the MHC molecule, optionally wherein the mutagenesis screen is a computational mutagenesis screen and those positions that are not involved in binding the MHC molecule are determined by a machine learning model, such as an artificial neural network, trained on peptide-MHC binding data; c) binding affinity to the MHC molecule, wherein peptides within the pool that are determined to have a binding affinity below a threshold binding affinity are not selected, optionallyAttorney Docket #: 250298.000961 wherein binding affinity is determined by a machine learning model, such as an artificial neural network, trained on peptide-MHC binding data; and d) tissue expression, wherein peptides within the pool that are not expressed in normal tissue, optionally not in essential normal tissue, are not selected.

47. The method of claim 46, wherein the proteome is a human proteome and the normal tissue or essential tissue is human tissue.

48. The method of any one of claims 44-47, wherein the high sequence similarity peptides include at least two amino acids that (i) are located at positions corresponding to positions within the target peptide that are available to interact with an antigen-recognition molecule and (ii) are identical to the corresponding amino acids of the target peptide.

49. A method of ranking a plurality of potential off-target peptides of a target peptide, the method comprising: obtaining a 3D computational model of a target peptide in complex with the MHC molecule (“MHC-target model”); obtaining a plurality of off target 3D computational models of a potential off-target peptide in a groove of an MHC molecule (“comparison MHC-off-target models”) such that each of the plurality of off-target peptides is respectively represented in one or more comparison MHC-off- target models of the plurality of comparison MHC-off-target models; computing a structural similarly metric for each of the plurality of off-target peptides such that the structural similarity metric indicates a degree of similarity between the MHC-target model and at least a portion of the one or more comparison MHC-off-target models associated with the respective potential off-target peptide; and ranking the plurality of potential off-target peptides based at least in part on the structural similarity metric.

50. The method of claim 49, wherein obtaining the plurality of comparison MHC-off-target models comprises providing one or more comparison MHC-off-target models of the plurality of comparison MHC-off-target models according to the method of any one of claims 1-13.Attorney Docket #: 250298.000961 51. The method of claim 49 or 50, wherein computing the structural similarity metric for each of the plurality of off-target peptides comprises quantifying structural similarity between a potential off-target peptide of the plurality of off-target peptides in a groove of an MHC molecule and a target peptide in complex with the MHC molecule for the purposes of antigen-recognition molecule binding according to the method of any one of claims 21-43.

52. The method of any one of claims 49-51, further comprising: identifying high sequence similarity and structurally similar off-target peptide(s), from the plurality of potential off-target peptides, for an antigen-recognition molecule that recognizes an MHC-target peptide complex, according to the method of any one of claims 44-48; and ranking the high sequence similarity and structurally similar off-target peptide(s) based at least in part on the structural similarity metric.

53. The method of any one of claims 49-52, further comprising: providing a portion of the plurality of potential off-target peptides for in vitro assessment of off-target affects of an antigen-recognition model based at least in part on the ranking.

54. The method of any one of claims 49-52, further comprising: providing the ranking of the plurality of potential off-target peptides in a database.

55. The method of any one of claims 49-53, further comprising: selecting off-target peptides from the plurality of potential off-target peptides based on the ranking; and providing a list of the selected off-target peptides in a database with an association to the target peptide.

56. A method for ranking potential target peptides to mitigate off-target toxicity, the method comprising: obtaining two or more potential target peptides among disease-associated peptides that are predicted to bind to an MHC molecule;Attorney Docket #: 250298.000961 obtaining, for each of the potential target peptides, a respective list of potential off-target peptides; ranking, for each of the potential target peptides, potential off-target peptides within the respective list of off-target peptides based at least in part on structural similarity of each potential off-target peptide to the potential target peptide; and ranking the two or more potential target peptides based at least in part on the ranking of potential off-target peptides within the respective list of potential off-target peptides.

57. The method of claim 56, wherein obtaining, for each of the potential target peptides, a respective list of potential off-target peptides comprises identifying the high sequence similarity and structurally similar off-target peptide(s) according to the method of any one of claims 44-48.

58. The method of claim 56 or 57, wherein ranking, for each of the potential target peptides, potential off-target peptides within the respective list of off-target peptides comprises ranking the off-target peptide(s) according to the method of any one of claims 49-55.

59. The method of claim 58, further comprising: determining, for each of the two or more potential target peptides, a number structurally similar off-target peptide(s) based at least in part on a comparison of the highest ranked potential off-target peptide(s) associated with each of the potential target peptides; and ranking the two or more potential target peptides based at least in part on the number of structurally similar off-target peptide(s).

60. A method of ranking a plurality of potential off-target peptides for a target peptide, the method comprising: providing a target conformation, wherein the target conformation is a computational representation of a three-dimensional structure comprising the target peptide and a groove of a major histocompatibility complex (MHC) molecule, wherein the target peptide is positioned within the groove for binding to the MHC molecule; providing a plurality of off-target conformations, wherein each off-target conformation is a computational representation of a three-dimensional structure comprising a potential off-targetAttorney Docket #: 250298.000961 peptide and the groove of the MHC molecule and wherein each of the off-target conformations corresponds to one of the plurality of potential off-target peptides positioned within the groove for binding to the MHC molecule; aligning the target conformation with each of the off-target conformations in three- dimensional space; computing a difference value for each of the off-target conformations, wherein each difference value quantifies a difference between the target conformation and one of the off-target conformations; and ranking the plurality of off-target conformations based on their respective difference values.

61. The method of claim 60, wherein the difference values quantify distances between atoms of the target conformation and corresponding atoms of each of the off-target conformations, optionally wherein the difference values are average distances such as root mean square deviations (RMSDs).

62. The method of claim 61, wherein the difference values quantify distances between heavy atoms only.

63. The method of claim 61 or 62, wherein the distances comprise the distances between all heavy atoms of the target peptide backbone and all corresponding heavy atoms of each of the potential off-target peptide backbones.

64. The method of claim 61 or 62, wherein the distances consist of the distances between atoms, optionally all heavy atoms, of the target peptide backbone at each position that has been determined to be available for binding by an antigen-recognizing molecule to a peptide-MHC (pMHC) complex comprising the target peptide bound to the HLA molecule and all corresponding atoms of the potential off-target peptide backbones at each of the corresponding positions, optionally wherein the positions available for binding an antigen-recognizing molecule have been predicted by a mutagenesis screen to be those positions that, based on changes in binding affinity, are notAttorney Docket #: 250298.000961 involved in binding the MHC molecule, optionally wherein the mutagenesis screen is a computational mutagenesis screen and those positions that are not involved in binding the MHC molecule are determined by a machine learning model, such as an artificial neural network, trained on peptide-MHC binding data.

65. The method of claim 63, wherein the distances consist of the distances between all heavy atoms of the target peptide backbone and all corresponding heavy atoms of each of the potential off- target peptide backbones.

66. The method of claim 63, wherein the distances comprise the distances between heavy atoms of at least a portion of the groove of the MHC molecule in the target conformation and a corresponding portion of the groove of the MHC molecule in each of the off-target conformations, optionally wherein the portion comprises the bed and rails of the groove.

67. The method of claim 66, wherein the portion consists of the bed and the rails of the groove.

68. The method of claim 60, wherein the difference value quantifies a correlation between a molecular surface interaction fingerprint of the target conformation and each of the off-target conformations, wherein the molecular surface interaction fingerprint characterizes an interaction probability of the three-dimensional structure with an antigen-binding molecule based on one or more surface features, wherein the one or more surface features comprise geometric features and / or chemical features of the surface, optionally wherein the molecular surface interaction fingerprint is a vector, optionally wherein the difference value is a correlation coefficient such as a Pearson correlation coefficient, optionally wherein the geometric features comprise shape index or distance-dependent curvature and / or the chemical features comprise hydropathy, continuum electrostatics, or location of free electrons and proton donors.

69. The method of claim 68, wherein the molecular surface interaction fingerprint is a vector of interaction scores, wherein each interaction score is associated with a spatially localized portion of the molecular surface of the respective model and is a scalar value representative of a probabilityAttorney Docket #: 250298.000961 of the respective spatially localized portion being involved in a protein-protein interaction, optionally wherein each spatially localized portion is one of a plurality of overlapping patches that encompass the entire molecular surface of the respective model, further optionally wherein the vector comprises an interaction score for each patch of the plurality of patches.

70. The method of claim 69, wherein each patch of the plurality of overlapping patches is a geodesic patch having a fixed geodesic distance from a patch center, optionally wherein the patch center is a vertex of the molecular surface of the respective model and optionally wherein each patch has the same fixed geodesic distance.

71. The method of any one of claims 68-70, wherein the molecular surface interaction fingerprints are determined, at least in part, by geometric deep learning, optionally using convolutional neural network.

72. The method of any one of claims 68-71, wherein the molecular surface interaction fingerprints for each three-dimensional structure are determined by: a) decomposing a surface of the three-dimensional structure into a plurality of overlapping geodesic patches; b) mapping the one or more surface features of the three-dimensional structure to each of the geodesic patches using polar geodesic coordinates, wherein the one or more surface features comprise one or more, optionally all, of the following features: shape index, distance-dependent curvature, hydropathy, continuum electrostatics, and location of free electrons and proton donors; c) applying a convolutional neural network to each patch to produce an interaction score for each patch, wherein applying the convolutional neural network comprises rotating the geodesic patch to provide rotation invariance, and wherein the convolutional neural network has been trained on i) portions of surfaces that form interface regions between pairs of proteins that are known binding partners and ii) portions of surfaces that do not form interface regions between pairs of proteins, optionally wherein the interface regions are solvent inaccessible regions in complexes of the known binding partners and optionally wherein the proportions of surfaces that do not form interface regions are derived from one or both of the known binding partners; andAttorney Docket #: 250298.000961 d) determining the molecular surface interaction fingerprints based on the interaction scores of the plurality of overlapping geodesic patches, wherein determining the molecular surface interaction fingerprint comprises identifying spatially corresponding patches between the MHC- target model and each respective MHC off-target model and wherein the molecular surface interaction fingerprint comprises the interaction scores for the corresponding patches, optionally wherein determining the molecular surface interaction fingerprint comprises removing interaction scores that are not associated with a corresponding patch.

73. The method of any one of claims 72, wherein mapping the surface features to the geodesic patches comprises locally averaging the one or more surface features to learnable Gaussian kernels.

74. The method of any one of claims 60-73, wherein the plurality of potential off-target peptides, are selected from a list of peptides derivable from a proteome based on one or more of the following: a) a degree of similarity with the target peptide sequence, optionally wherein a threshold degree of similarity for selection requires one or more residue mismatches and / or requires one or more identical residues; b) a number of identical residues, optionally at least three, at positions within the target peptide sequence that have been determined to be available for binding by an antigen-recognizing molecule to a peptide-MHC (pMHC) complex comprising the target peptide bound to the HLA molecule, optionally wherein the positions available for binding an antigen-recognizing molecule have been predicted by a mutagenesis screen to be those positions that, based on changes in binding affinity, are not involved in binding the MHC molecule, optionally wherein the mutagenesis screen is a computational mutagenesis screen and those positions that are not involved in binding the MHC molecule are determined by a machine learning model, such as an artificial neural network, trained on peptide-MHC binding data; c) binding affinity to the MHC molecule, wherein peptides that are determined to have a binding affinity below a threshold binding affinity are not selected, optionally wherein bindingAttorney Docket #: 250298.000961 affinity is determined by a machine learning model, such as an artificial neural network, trained on peptide-MHC binding data; and d) tissue expression, wherein peptides that are not expressed in normal tissue, optionally not in essential normal tissue, are not selected.

75. The method of claim 74, wherein the proteome is a human proteome and the normal tissue or essential normal tissue is human tissue.

76. The method of any one of claims 60-75, wherein the three-dimensional structure of the target conformation and / or the three-dimensional structures of one or more, optionally all, of the plurality of off-target conformations have been determined, at least in part, from a predicted structure determined using one or more of the following: a) template-based modeling; b) sequence-based machine learning; and / or c) experimental measurements, optionally wherein the experimental measurements are made using X-ray crystallography or Cryo-electron microscopy (Cryo-EM).

77. The method of claim 76, wherein the predicted structure(s) has been determined by a template- based modeling process comprising: a) searching a database of known protein structures comprising a template peptide bound to the MHC molecule to identify a plurality of template structures based, at least in part, on sequence similarity of the template peptide with the peptide sequence of the target peptide or potential off-target peptide; b) aligning the peptide sequence to each of the three-dimensional structures of the template structures based on a comparison of the sequences; c) calculating an energy score for each of the aligned peptide sequences; d) selecting a template structure based on the calculated energy scores; and e) assigning a predicted structure based on the selected template structure.Attorney Docket #: 250298.000961 78. The method of claim 75 or 76, wherein the predicted structure(s) has been determined by sequence-based machine learning, optionally wherein the sequence-based machine learning uses a neural network-based model.

79. The method of any one claims 60-78, wherein the three-dimensional structure of the target conformation and / or the three-dimensional structures of one or more, optionally all, of the plurality of off-target conformations have been determined, at least in part, from a prepacked predicted structure, wherein the prepacked predicted structure is optimized based at least in part on the selection of rotamer combinations for the peptide and MHC molecule to eliminate steric clashes, optionally wherein the predicted structure is determined using templated-based modeling or experimental measurements followed by prepacking.

80. The method of any one of claims 60-79, wherein the three-dimensional structure of the target conformation and the three-dimensional structures of all of the plurality of off-target conformations have been determined, at least in part, from predicted structures determined using the same approach, optionally template-based modeling or sequence-based machine learning.

81. The method of any one of claims 60-80, wherein the three-dimensional structure of the target conformation has been refined from an initial three-dimensional structure by a computational peptide docking algorithm, optionally wherein the initial three-dimensional structure is a predicted structure of any one of claims 14-18, optionally wherein the predicted structure is a prepacked predicted structure.

82. The method of any one claims 60-81, wherein the three-dimensional structure of one or more, optionally all, of the plurality of off-target conformations have been refined from initial three- dimensional structures by a computational peptide docking algorithm, optionally wherein the initial three-dimensional structure is a predicted structure of any one of claims 14-18, optionally wherein the predicted structure is a prepacked predicted structure.Attorney Docket #: 250298.000961 83. The method of claim 81 or 82, wherein the computational peptide docking algorithm comprises a Monte Carlo search with minimization algorithm.

84. The method of any one of claims 81-83, wherein the computational peptide docking algorithm comprises the following steps: a) modifying an energy function used to evaluate the three-dimensional structure by reducing the weight of van der Waals repulsive forces and / or increasing the weight of van der Waals attractive forces, optionally both, to an extent that will permit sampling of alternative conformations of the peptide within the groove while preventing the peptide from separating from a binding pocket within the groove of the MHC molecule during a subsequent energy minimization reconfiguration of the three-dimensional structure; b) optimizing the rigid body orientation by applying a random rigid body perturbation, optionally a Gaussian rigid body perturbation, comprising a rotation and / or translation to affect the orientation of the peptide within the three-dimensional structure with respect to the groove, repacking the side chains of rotamers within the peptide-MHC interface following the random rigid body perturbation, and applying an energy minimization step following the repacking to arrive at a reconfigured rigid body orientation, wherein the repacking comprises optimizing the selection of rotamer combinations for the peptide-MHC interface to eliminate steric clashes, wherein the energy minimization step comprises using a deterministic algorithm to find a local energy minimum, wherein the reconfigured rigid body orientation is accepted only if an energy function criterion, optionally the Metropolis criterion, is met, and wherein the applying of the random rigid body perturbation, the repacking, and the energy minimization step are sequentially repeated for a plurality of cycles, optionally a predefined number of cycles and / or until an energy criterion is satisfied; c) optimizing the peptide backbone conformation, following optimization of the rigid body orientation, by applying a random torsion angle perturbation to the peptide backbone, optionally comprising a Rosetta small move or a Rosetta shear move, repacking the side chains of rotamers within the peptide-MHC interface following the random torsion angle perturbation, and applying an energy minimization step following the repacking to arrive at a reconfigured peptide backbone conformation, wherein the repacking comprises optimizing the selection of rotamer combinationsAttorney Docket #: 250298.000961 for the peptide-MHC interface to eliminate steric clashes, wherein the energy minimization step comprises using a deterministic algorithm to find a local energy minimum, wherein the reconfigured peptide backbone conformation is accepted only if an energy function criterion, optionally the Metropolis criterion, is met, and wherein the applying of the random torsion angle perturbation, the repacking, and the energy minimization step are sequentially repeated for a plurality of cycles, optionally a predefined number of cycles and / or until an energy criterion is satisfied, optionally wherein the random torsion angle perturbation alternates between Rosetta small moves and Rosetta shear moves each cycle; and e) repeating steps (b) and (c) for a plurality of cycles wherein the van der Waals forces are gradually ramped back towards normal values such that the last cycle is performed with the normal values to arrive at a refined three-dimensional structure.

85. The method of any one of claims 81-84, wherein the computational peptide docking algorithm is repeated a plurality of times, optionally at least 100, 200, 500, 1,000, 2,000, 5,000, or 10,000 times, to produce a plurality of refined three-dimensional structures and wherein ranking the plurality of off-target conformations based on their respective difference values comprises ranking the plurality of off-target conformations based on an aggregate measure of the computed difference values for at least several of the plurality of refined three-dimensional structures.

86. The method of claim 85, wherein the at least several of the plurality of refined three- dimensional structures consist of a predetermined number, optionally at least 5, of the refined three-dimensional structures having the lowest energy scores as evaluated by an energy function.

87. The method of claim 84 or 85, wherein the aggregate measure comprises an average, median, or minimum.

88. The method of claim 86 or 87, wherein each energy score comprises a total energy score for the refined three-dimensional structure, an interface score that measures an energy of pairwise interactions across a peptide-MHC interface, a peptide score that measures an energy function over the residues of the peptide, or a combination thereof, optionally a weighted sum.Attorney Docket #: 250298.000961 89. A non-transitory computer-readable medium configured to communicate with one or more processor(s) of a computational device, the non-transitory computer-readable medium including instructions thereon, that when executed by the processor(s), cause the computational device to perform the method of any one of claims 1-88.

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