218results about "Peptide libraries" patented technology

Provided herein are methods for capturing an analyte from a first region of interest of a biological sample on a substrate, where the biological sample comprises the first region of interest and a second region, and where the method includes contacting the second region with a sealant in order to create a hydrophobic seal thereby preventing an interaction between an analyte from the second region with a capture domain of a capture probe.

Methods for preparing a personalized cancer vaccine and a method to train a machine learning HLA-peptide presentation prediction model. Further wherein, a method of making a HLA class II tetramer or multimer comprising an epitope, the method comprising contacting a purified soluble HLA-DM loaded with a peptide epitope with a HLA class II tetramer or multimer, thereby forming a HLA class II tetramer or multimer loaded with the peptide epitope, is disclosed.

A method for analyzing macromolecules, including peptides, polypeptides, and proteins, employing nucleic acid encoding is disclosed.

VH domain, in which: (i) the amino acid residue at position 112 is one of K or Q; and / or (ii) the amino acid residue at position 89 is T; and / or (iii) the amino acid residue at position 89 is L and the amino acid residue at position 110 is one of K or Q; and (iv) in each of cases (i) to (iii), the amino acid at position 11 is preferably V; and in which said VH domain contains a C-terminal extension (X)n, in which n is 1 to 10, preferably 1 to 5, such as 1, 2, 3, 4 or 5 (and preferably 1 or 2, such as 1); and each X is an (preferably naturally occurring) amino acid residue that is independently chosen, and preferably independently chosen from the group consisting of alanine (A), glycine (G), valine (V), leucine (L) or isoleucine (I).

To provide a method for introducing a nucleic acid into a floating cell.SOLUTION: The present invention provides a method for introducing nucleic acids into non-adherent cells, comprising the step of contacting nucleic acids with non-adherent cells in solutions comprising dextran derivatives having average molecular weights greater than 70kDa.SELECTED DRAWING: None

The invention discloses DNA (deoxyribonucleic acid) coupled non-natural amino acid as well as a synthesis method and application thereof. The synthesis method of the DNA coupled non-natural amino acid comprises the following steps: adding inorganic alkali and 2, 5-dibromohexane diamide into a boric acid buffer solution containing DNA coupled cysteine as shown in a general formula (I) in the specification, adding an organic phase, and reacting at 25-37 DEG C to enable the DNA coupled cysteine to be subjected to desulfurization elimination, thereby obtaining the DNA coupled non-natural amino acid. DNA coupling dehydroalanine shown as a general formula (II) in the specification is obtained; the method comprises the following steps: carrying out nucleophilic addition reaction on DNA coupled dehydroalanine and a nucleophilic reagent under an alkaline condition or carrying out dipolar cycloaddition reaction on DNA coupled dehydroalanine and 2, 5-substituted tetrazole under an ultraviolet condition to obtain the DNA coupled unnatural amino acid. By adopting the method, the integrity of the DNA chain can be effectively ensured, no by-product is generated in the reaction, and a more powerful chemical tool is provided for construction and subsequent modification of a DNA coding molecular library.

The present disclosure relates to a modified polypeptide of glutamine synthetase having enhanced activity and a method of producing L-glutamine using the same. Since production of L-glutamine may be increased by using the novel modified polypeptide without a decrease in a growth rate compared to wild-type strains having glutamine synthetase activity, the modified polypeptide may be widely used for mass production of L-glutamine.

Disclosed is a peptide-immobilized bead library from which peptides are more likely to be obtained as candidates of useful substances such as pharmaceuticals, and with which the amino acid sequence bound to a target substance can be more easily analyzed, compared to known OPOB libraries. The peptide-immobilized bead library has a structure of General Formula [I]. In General Formula [I], X is an amino acid residue; n is an integer of 4 to 8; Y is a cyclization structure; A is a spacer structure; B is a specific cleavage site-containing structure; and the 4 to 8 amino acid residues of X are each independently randomly selected.

The present invention relates to methods for producing recombinant binding proteins with binding specificity for peptide-MHC (pMHC) complexes. The invention also relates to recombinant binding proteins with binding specificity for pMHC complexes, which comprise one, two or more designed repeat domains, preferably designed ankyrin repeat domains, and to such binding proteins which further comprise a binding factor with binding specificity for a protein expressed on the surface of immune cells, preferably T cells. In addition, the invention relates to nucleic acids encoding such binding proteins or repeat domains, pharmaceutical compositions comprising such binding proteins or nucleic acids, and the use of such binding proteins, nucleic acids or pharmaceutical compositions in methods for treating or diagnosing diseases, including cancer, infectious diseases and autoimmune diseases.

The present invention provides a cyclic peptide compound optionally linked to a nucleic acid, the cyclic peptide compound having a cyclic moiety wherein: (1) the cyclic moiety is composed of 13 or 14 amino acid residues; (2) among the amino acid residues constituting the cyclic moiety, the number of N-substituted amino acid residues is 7 or more, the number of amino acid residues in a single side chain is 3 or fewer, and the number of native amino acid residues is 4 or fewer; and (3) the ClogP / total amide bond (ClogP / total AB) is 1.0 to 1.8.

Described herein are VHH antibody libraries with heavy chain variable domain framework scaffolds that have complementarity determining regions (CDRs) found in naturally occurring human antibodies, and methods for making such antibody libraries. The antibody libraries do not include members that contain one or more liabilities that affect one or more properties of the members.

The present invention relates to a method of selecting a polypeptide for display on a genetic display system according to activity, comprising the steps of: displaying the polypeptide on the genetic display system, screening a system for binding to a target, and selecting a member binding to the target; cloning a nucleic acid encoding the polypeptide from a member of the display system, and expressing the nucleic acid in an expression system to produce the polypeptide, or sequencing the polypeptide from a member of the display system, and cloning and expressing the polypeptide or a library of polypeptides using synthesis-based DNA; and determining the activity of the polypeptide in an assay.

Use of a compound, microarray chip substrate, microarray chip and use and method thereof. The present application provides use of a compound, or a geometric isomer, tautomer, isotopically labeled, hydrate, solvate or salt thereof in chip surface modification. Also provided is a microarray chip substrate modified by the compound, and a microarray chip comprising the microarray chip substrate. The microarray chip substrate of the present application can greatly improve the surface modification function by surface modification, improve nucleic acid synthesis yield, amplify detection signal, and avoid non-specificity and cross-talk. It has a wide application prospect.

The present invention provides a method for constructing a cyclic compound library that overcomes the limitations of conventional ring-closing methods for cyclic compound libraries, has the advantages of milder ring-closing reaction conditions and high generality, can be used to construct monocyclic and bicyclic compound libraries, and involves few side reactions. [Solution] A cyclic compound library and its construction method are provided, which uses a solid support, a molecule containing a photocleavable group, a linker, a building block, a ring-closing A-terminal molecule, and a ring-closing B-terminal molecule at both ends of the reaction synthesis, and utilizes the decomposition of the solid support under light irradiation to complete ring closure of the amino acid residue structures of the ring-closing A-terminal molecule A and the ring-closing B-terminal molecule B through the action of cyclohydrolase. This method, which uses mild ring closure conditions, is more universal and expands the types of chemical reactions and the diversity of the encoded compound library.

The present invention provides methods for evaluation of potential tumor neoepitopes to assess the probability that they constitute immunogenic neoantigens in a cancer affected subject. The present invention provides vaccines comprising immunogenic neoepitopes for treatment of cancer in subjects in need thereof, optionally with the coadministration of cathepsin inhibitor.

Provided are methods comprising expressing in a recombinant cell comprising a Cas gene a recombinant error-prone reverse transcriptase (RT) and a recombinant spacer RNA comprising a target sequence for mutagenesis of a DNA sequence in the Cas gene; making a mutagenized cDNA polynucleotide homologous to the DNA sequence in the recombinant cell; expressing a recombinant recombineering system in the recombinant cell; and recombining the mutagenized cDNA with the homologous DNA sequence of the Cas gene in the recombinant cell. Also provided are recombinant cells comprising recombinant coding sequences for a recombinant Cas protein, recombinant error-prone reverse transcriptase (RT), recombinant spacer RNA comprising the target sequence, and recombinant recombineering system.

Provided are 3-4 residue non-natural macrocyclic oligoamides comprising species of 3 or 4 monomer residues selected from the group consisting of monomers a, b, c, d, e, f, g, h, I, j, k, l, m, n, o, p, q, r, s, t, u, and v as defined in Table 1, and methods for designing such macrocyclic oligoamides.

The invention features base editors having reduced non-target deamination, methods of using the base editors, and assays for characterizing base editors as having decreased non-target deamination, e.g. compared to programmed, on-target deamination.

An extracellular vesicle (EV) associated with a viral vector is provided. The combination of the EV and virus vectors provide widespread and highly efficient transgene expression in lungs, following localized administration, as well as in mucus-covered air-liquid interface (ALI) cultures with primary human bronchial epithelial (HBE) cells and nasal epithelial (HNE) cells.

Provided herein are systems and methods for screening desirable biological variants using a high-throughput integrated system. The integrated system may be configured to input a plurality of parameters from functional studies of biological variants under applied conditions, in conjunction with integrated libraries of biological variants, and filter the inputs to produce desirable biological variants based on an input performance requirement. The system may output optimized strains, molecules, or novel molecules expected to have a desirable functional characteristic. Accordingly, the methods and systems disclosed herein enable multi-parametric studies of biological diversity and conditional diversity in systems biology.

It provides an improved immunoglobulin variable domain. [Solution] A VH domain comprising: (i) the amino acid residue at position 112 is either K or Q, and / or; (ii) the amino acid residue at position 89 is T, and / or; (iii) the amino acid residue at position 89 is L, the amino acid residue at position 110 is either K or Q, and (iv) in each of (i) to (iii), the amino acid at position 11 is preferably V, and the VH domain contains a C-terminal extension (X)n [wherein n is 1 to 10, preferably 1 to 5, for example 1, 2, 3, 4, or 5, and each X is a (preferably native) amino acid residue, independently selected from alanine (A), glycine (G), valine (V), leucine (L), or isoleucine (I), preferably independently selected from the group consisting of these].

The invention discloses a polypeptide for inducing immune myocarditis and application of the polypeptide. The polypeptide comprises an amino acid sequence as shown in at least one of SEQ ID NO. 1 to SEQ ID NO. 39. The polypeptide has obvious immunogenicity and inflammatory potential, and can be used as a stable and repeatable immune myocarditis induction system.

An object of the present invention is to provide a novel cyclic peptide compound excellent in cell membrane permeability, a method for producing the same, a composition for screening use, and a method for selecting a cyclic peptide compound that binds to a target substance. According to the present invention, a peptide compound represented by Formula (1) or a salt thereof is provided. In the formula, the symbols have the meanings as defined in the specification of the present application.

Compositions of peptides modified to improve HLA binding or T cell recognition while conserving reactivity to the target neoepitope, enhance activation of neoantigen-specific T cells. Methods of use include treating cancer by administering one or more of these peptides generated by computer modeling.

A cysteine-directed proximity-driven strategy for the construction of bicyclic peptides from simple natural peptide precursors. This linear to bicycle transformation initiates with rapid cysteine labeling, which then triggers proximity-driven amine-selective cyclization. This bicyclization proceeds rapidly under physiologic conditions, yielding bicyclic peptides with a Cys-Lys-Cys, Lys-Cys-Lys or N-terminus-Cys-Cys stapling pattern. Novel phage libraries of bicyclic peptides and method of use thereof for screening therapeutic proteins.

The present disclosure relates to the development of a synthetic peptide library. This synthetic peptide library comprises at least about 1×10^3, 1×10^4, 1×10^5, 1×10^6, or 1×10^7 peptide sequences derived from a single reference sequence, wherein a subset of the derived peptide sequences comprises peptide sequences comprising a functional pharmacokinetic parameter (FPKP) delectably improved relative to the single reference sequence.

Disclosed is a method for producing a compound library comprising two or more cyclic compounds represented by the formula (I), comprising a step of allowing a macrocyclase in vitro to act on two or more peptides represented by the formula (II): LP-X—(Xa)m-Y—Z (II) wherein X represents a group represented by the formula (1), Y is a peptide residue consisting of four amino acids and / or analogs thereof and contains a group represented by the formula (2) (wherein R1 and B1 are as defined above, and R3 represents a hydrogen or a hydrocarbon group), and LP is present or absent and, when present, represents a peptide residue consisting of 1 to 100 amino acids and / or analogs thereof, and forming the nitrogen-containing 6-membered ring A while eliminating LP, if present, to form the two or more cyclic compounds represented by the formula (I).

The present disclosure provides a peptide library comprising stable isotope-labeled (SIL) peptides, wherein the peptides comprise or consist of the sequences according to Table A, Table B, or Table C.

Disclosed is a fluorescently labeled peptide library useful for diagnosing multiple sclerosis. The fluorescently labeled peptide library comprising fluorescently labeled peptides represented by the following formula:wherein X1, X2, X3 and X4 are independently arbitrary amino acid residues, and the peptides are immobilized on a chip.