Hydrogels comprising protein-stabilized nanoparticles for extended release

Abstract

The present disclosure provides compositions comprising a hydrogel and a protein-stabilized nanoparticle. The hydrogel comprises a crosslinked protein matrix, the protein-stabilized nanoparticle comprises a therapeutic agent or a diagnostic agent, and the protein-stabilized nanoparticle is embedded in the crosslinked protein matrix. The compositions thus provide a means of controlled and prolonged delivery of therapeutic and diagnostic agents. The present disclosure further provides kits comprising the compositions, methods of treating or preventing a disease or disorder, and methods of preparing the compositions.

Description

[0001]HYDROGELS COMPRISING PROTEIN-STABILIZED NANOPARTICLES FOR EXTENDED RELEASE RELATED APPLICATIONS This application claims priority under 35 U.S.C. § 119(e) to U.S. Provisional Application, U.S.S.N.63 / 609,239, filed December 12, 2023, which is incorporated herein by reference in its entirety. FEDERALLY SPONSORED RESEARCH This invention was made with government support under Grant Number GM131728, awarded by the National Institutes of Health. The Government has certain rights in the invention. BACKGROUND Effective pain management is essential for improving physical and mental functioning and reducing dependence on opioid medication. Local anesthetics are extremely effective at preventing the perception of pain when injected at a painful body location, or at a nerve leading to the site. However, one shortcoming is their relatively short duration of effect. For decades, investigators have been developing injectable sustained release systems to prolong that duration, investigating a wide range of vehicles. Initial interest was driven by the desire to alleviate pain and suffering, and to prevent physiological derangements associated with it. Since the advent of the opioid epidemic, interest in prolonged local anesthesia (PLA) has also been driven by the potential to replace opioids in the treatment of relatively localized pain (e.g., after shoulder surgery) for the duration of the perioperative period (a few days). The effect of conventional local anesthetics by injectable PLA systems is typically several fold, but – in the absence of adjunctive drugs such as glucocorticoid steroids – they rarely achieve even a day of nerve block in established models. As one example, in the animal model employed herein, the commercially available liposomal bupivacaine formulation EXPAREL®only provides 4-8 hours of nerve block. One important limitation in this regard is that conventional local anesthetics are relatively low in potency, which limits the effectiveness of the payload. Additionally, local anesthetics can cause inflammation at the site of injection, as well as injury to muscle and nerve. These toxicities can be worsened by sustained release, in a manner dependent on the level and duration of release. This toxicity can limit the duration of effect of systems releasing conventional local anesthetics. #13447332v2 SUMMARY The present disclosure describes the realization of hybrid particle-hydrogels that enable sustained release specifically at a site of application making them promising candidates for drug delivery. In one aspect, disclosed herein is a composition comprising a hydrogel and a protein- stabilized particle, wherein: the hydrogel comprises a crosslinked protein matrix; the protein-stabilized particle comprises a therapeutic agent or a diagnostic agent; and the protein-stabilized particle is embedded in the crosslinked protein matrix. In another aspect, provided are methods of treating a disease or condition, the method comprising administering an effective amount of the composition. In another aspect, provided are methods of preparing the composition, the method comprising: providing a therapeutic agent or a diagnostic agent; forming a protein-stabilized nanoparticle comprising the therapeutic agent or the diagnostic agent by exposing the therapeutic agent or the diagnostic agent to a solution of a protein in water; and reacting the protein with a crosslinking agent, thereby producing a crosslinked protein matrix. In another aspect, provided are kits comprising the composition and instructions for using the composition. The details of certain embodiments of the invention are set forth in the Detailed Description of Certain Embodiments, as described below. Other features, objects, and advantages of the invention will be apparent from the Definitions, Drawings, Examples, and Claims. DEFINITIONS Definitions of specific functional groups and chemical terms are described in more detail below. The chemical elements are identified in accordance with the Periodic Table of the Elements, CAS version, Handbook of Chemistry and Physics, 75thEd., inside cover, and specific functional groups are generally defined as described therein. Additionally, general principles of organic chemistry, as well as specific functional moieties and reactivity, are described in Thomas Sorrell, Organic Chemistry, University Science Books, Sausalito, 1999;Michael B. Smith, March’s Advanced Organic Chemistry, 7thEdition, John Wiley & Sons, Inc., New York, 2013; Richard C. Larock, Comprehensive Organic Transformations, John Wiley & Sons, Inc., #13447332v2 New York, 2018; and Carruthers, Some Modern Methods of Organic Synthesis, 3rdEdition, Cambridge University Press, Cambridge, 1987. Compounds described herein can comprise one or more asymmetric centers, and thus can exist in various stereoisomeric forms, e.g., enantiomers and / or diastereomers. For example, the compounds described herein can be in the form of an individual enantiomer, diastereomer, or geometric isomer, or can be in the form of a mixture of stereoisomers, including racemic mixtures and mixtures enriched in one or more stereoisomer. Isomers can be isolated from mixtures by methods known to those skilled in the art, including chiral high pressure liquid chromatography (HPLC) and the formation and crystallization of chiral salts; or preferred isomers can be prepared by asymmetric syntheses. See, for example, Jacques et al., Enantiomers, Racemates and Resolutions (Wiley Interscience, New York, 1981); Wilen et al., Tetrahedron 33:2725 (1977); Eliel, E.L. Stereochemistry of Carbon Compounds (McGraw–Hill, NY, 1962); and Wilen, S.H., Tables of Resolving Agents and Optical Resolutions p.268 (E.L. Eliel, Ed., Univ. of Notre Dame Press, Notre Dame, IN 1972). The disclosure additionally encompasses compounds as individual isomers substantially free of other isomers, and alternatively, as mixtures of various isomers. When a range of values is listed, it is intended to encompass each value and sub–range within the range. For example, “C1–6” is intended to encompass C1, C2, C3, C4, C5, C6, C1–6, C1–5, C1–4, C1–3, C1–2, C2–6, C2–5, C2–4, C2–3, C3–6, C3–5, C3–4, C4–6, C4–5, and C5–6. For example, “C1-6alkyl” encompasses, C1, C2, C3, C4, C5, C6, C1–6, C1–5, C1–4, C1–3, C1–2, C2–6, C2–5, C2–4, C2–3, C3– 6, C3–5, C3–4, C4–6, C4–5, and C5–6 alkyl. The term “alkyl” refers to a radical of a straight-chain or branched saturated hydrocarbon group having from 1 to 20 carbon atoms (“C1–20alkyl”). The term “branched alkyl” refers to a radical of a branched saturated hydrocarbon group having from 1 to 20 carbon atoms (“branched C1–20 alkyl”), for example, isopropyl, t-butyl, sec-butyl, iso-butyl, neopentyl, isopentyl, and neoheptyl. The term “unbranched alkyl” is the same as a straight-chain or linear alkyl group, i.e., an alkyl group having no alkyl branching groups. In some embodiments, an alkyl group has 1 to 12 carbon atoms (“C1–12 alkyl”). In some embodiments, an alkyl group has 1 to 10 carbon atoms (“C1–10alkyl”). In some embodiments, an alkyl group has 1 to 9 carbon atoms (“C1–9alkyl”). In some embodiments, an alkyl group has 1 to 8 carbon atoms (“C1–8 alkyl”). In some embodiments, an alkyl group has 1 to 7 carbon atoms (“C1–7 alkyl”). In some embodiments, an alkyl group has 1 to 6 carbon atoms (“C1–6alkyl”). In some embodiments, an alkyl group has 1 to 5 carbon atoms (“C1–5alkyl”). In some embodiments, an alkyl group has 1 to 4 carbon atoms (“C1–4 alkyl”). In some embodiments, an alkyl group has 1 to 3 carbon atoms (“C1–3 alkyl”). In some embodiments, an alkyl group has 1 to 2 carbon atoms (“C1–2 alkyl”). In some #13447332v2 embodiments, an alkyl group has 1 carbon atom (“C1 alkyl”). In some embodiments, an alkyl group has 2 to 6 carbon atoms (“C2-6alkyl”). Examples of C1–6alkyl groups include methyl (C1), ethyl (C2), propyl (C3) (e.g., n-propyl, isopropyl), butyl (C4) (e.g., n-butyl, tert-butyl, sec-butyl, isobutyl), pentyl (C5) (e.g., n-pentyl, 3-pentanyl, amyl, neopentyl, 3-methyl-2-butanyl, tert- amyl), and hexyl (C6) (e.g., n-hexyl). Additional examples of alkyl groups include n-heptyl (C7), n-octyl (C8), n-dodecyl (C12), and the like. Unless otherwise specified, each instance of an alkyl group is independently unsubstituted (an “unsubstituted alkyl”) or substituted (a “substituted alkyl”) with one or more substituents (e.g., halogen, such as F). In certain embodiments, the alkyl group is an unsubstituted C1–12alkyl (such as unsubstituted C1–6alkyl, e.g., −CH3(Me), unsubstituted ethyl (Et), unsubstituted propyl (Pr, e.g., unsubstituted n-propyl (n-Pr), unsubstituted isopropyl (i-Pr)), unsubstituted butyl (Bu, e.g., unsubstituted n-butyl (n-Bu), unsubstituted tert-butyl (tert-Bu or t-Bu), unsubstituted sec-butyl (sec-Bu or s-Bu), unsubstituted isobutyl (i-Bu)). In certain embodiments, the alkyl group is a substituted C1–12alkyl (such as substituted C1–6 alkyl, e.g., –CH2F, –CHF2, –CF3, –CH2CH2F, –CH2CHF2, –CH2CF3, or benzyl (Bn)). The term “alkenyl” refers to a radical of a straight-chain or branched hydrocarbon group having from 1 to 20 carbon atoms and one or more carbon-carbon double bonds (e.g., 1, 2, 3, or 4 double bonds). In some embodiments, an alkenyl group has 1 to 20 carbon atoms (“C1-20 alkenyl”). In some embodiments, an alkenyl group has 1 to 12 carbon atoms (“C1–12alkenyl”). In some embodiments, an alkenyl group has 1 to 11 carbon atoms (“C1–11 alkenyl”). In some embodiments, an alkenyl group has 1 to 10 carbon atoms (“C1–10 alkenyl”). In some embodiments, an alkenyl group has 1 to 9 carbon atoms (“C1–9alkenyl”). In some embodiments, an alkenyl group has 1 to 8 carbon atoms (“C1–8alkenyl”). In some embodiments, an alkenyl group has 1 to 7 carbon atoms (“C1–7 alkenyl”). In some embodiments, an alkenyl group has 1 to 6 carbon atoms (“C1–6 alkenyl”). In some embodiments, an alkenyl group has 1 to 5 carbon atoms (“C1–5alkenyl”). In some embodiments, an alkenyl group has 1 to 4 carbon atoms (“C1–4alkenyl”). In some embodiments, an alkenyl group has 1 to 3 carbon atoms (“C1–3 alkenyl”). In some embodiments, an alkenyl group has 1 to 2 carbon atoms (“C1–2 alkenyl”). In some embodiments, an alkenyl group has 1 carbon atom (“C1alkenyl”). The one or more carbon- carbon double bonds can be internal (such as in 2-butenyl) or terminal (such as in 1-butenyl). Examples of C1–4 alkenyl groups include methylidenyl (C1), ethenyl (C2), 1-propenyl (C3), 2- propenyl (C3), 1-butenyl (C4), 2-butenyl (C4), butadienyl (C4), and the like. Examples of C1–6alkenyl groups include the aforementioned C2-4alkenyl groups as well as pentenyl (C5), pentadienyl (C5), hexenyl (C6), and the like. Additional examples of alkenyl include heptenyl (C7), octenyl (C8), octatrienyl (C8), and the like. Unless otherwise specified, each instance of an #13447332v2 alkenyl group is independently unsubstituted (an “unsubstituted alkenyl”) or substituted (a “substituted alkenyl”) with one or more substituents. In certain embodiments, the alkenyl group is an unsubstituted C1-20alkenyl. In certain embodiments, the alkenyl group is a substituted C1-20alkenyl. In an alkenyl group, a C=C double bond for which the stereochemistry is not specified -configuration. or branched hydrocarbon group having from 1 to 20 carbon atoms and one or more carbon-carbon triple bonds (e.g., 1, 2, 3, or 4 triple bonds) (“C1-20alkynyl”). The term “linear alkynyl” refers to a radical of a straight-chain, unbranched hydrocarbon group having from 1 to 20 carbon atoms and one or more carbon- carbon triple bonds (e.g., 1, 2, 3, or 4 triple bonds) (“C1-20 alkynyl”). In some embodiments, an alkynyl group has 1 to 10 carbon atoms (“C1-10alkynyl”). In some embodiments, an alkynyl group has 1 to 9 carbon atoms (“C1-9alkynyl”). In some embodiments, an alkynyl group has 1 to 8 carbon atoms (“C1-8 alkynyl”). In some embodiments, an alkynyl group has 1 to 7 carbon atoms (“C1-7alkynyl”). In some embodiments, an alkynyl group has 1 to 6 carbon atoms (“C1-6alkynyl”). In some embodiments, an alkynyl group has 1 to 5 carbon atoms (“C1-5alkynyl”). In some embodiments, an alkynyl group has 1 to 4 carbon atoms (“C1-4 alkynyl”). In some embodiments, an alkynyl group has 1 to 3 carbon atoms (“C1-3 alkynyl”). In some embodiments, an alkynyl group has 1 to 2 carbon atoms (“C1-2alkynyl”). In some embodiments, an alkynyl group has 2 to 10 carbon atoms (“C2–10alkynyl”). In some embodiments, an alkynyl group has 2 to 9 carbon atoms (“C2–9 alkynyl”). In some embodiments, an alkynyl group has 2 to 8 carbon atoms (“C2–8alkynyl”). In some embodiments, an alkynyl group has 2 to 7 carbon atoms (“C2–7alkynyl”). In some embodiments, an alkynyl group has 2 to 6 carbon atoms (“C2–6alkynyl”). In some embodiments, an alkynyl group has 2 to 5 carbon atoms (“C2–5 alkynyl”). In some embodiments, an alkynyl group has 2 to 4 carbon atoms (“C2–4alkynyl”). In some embodiments, an alkynyl group has 2 to 3 carbon atoms (“C2–3alkynyl”). In some embodiments, an alkynyl group has 2 carbon atoms (“C2 alkynyl”). In some embodiments, an alkynyl group has 1 carbon atom (“C1 alkynyl”). The one or more carbon-carbon triple bonds can be internal (such as in 2- butynyl) or terminal (such as in 1-butynyl). Examples of C1-4alkynyl groups include, without limitation, methylidynyl (C1), ethynyl (C2), 1-propynyl (C3), 2-propynyl (C3), 1-butynyl (C4), 2- butynyl (C4), and the like. Examples of C1-6 alkenyl groups include the aforementioned C2-4 alkynyl groups as well as pentynyl (C5), hexynyl (C6), and the like. Examples of C2–4alkynyl groups include, without limitation, ethynyl (C2), 1–propynyl (C3), 2–propynyl (C3), 1–butynyl (C4), 2–butynyl (C4), and the like. Examples of C2–6 alkenyl groups include the aforementioned C2–4alkynyl groups as well as pentynyl (C5), hexynyl (C6), and the like. Additional examples of alkynyl include heptynyl (C7), octynyl (C8), and the like. Unless otherwise specified, each #13447332v2 instance of an alkynyl group is independently unsubstituted (an “unsubstituted alkynyl”) or substituted (a “substituted alkynyl”) with one or more substituents. In certain embodiments, the alkynyl group is an unsubstituted C1-20alkynyl. In certain embodiments, the alkynyl group is a substituted C1-20 alkynyl. In certain embodiments, the alkynyl group is an optionally substituted C2-20 alkynyl. The term “carbocyclyl” or “carbocyclic” refers to a radical of a non-aromatic cyclic hydrocarbon group having from 3 to 14 ring carbon atoms (“C3-14 carbocyclyl”) and zero heteroatoms in the non-aromatic ring system. In some embodiments, a carbocyclyl group has 3 to 14 ring carbon atoms (“C3-14carbocyclyl”). In some embodiments, a carbocyclyl group has 3 to 13 ring carbon atoms (“C3-13 carbocyclyl”). In some embodiments, a carbocyclyl group has 3 to 12 ring carbon atoms (“C3-12 carbocyclyl”). In some embodiments, a carbocyclyl group has 3 to 11 ring carbon atoms (“C3-11carbocyclyl”). In some embodiments, a carbocyclyl group has 3 to 10 ring carbon atoms (“C3-10carbocyclyl”). In some embodiments, a carbocyclyl group has 3 to 8 ring carbon atoms (“C3-8 carbocyclyl”). In some embodiments, a carbocyclyl group has 3 to 7 ring carbon atoms (“C3-7 carbocyclyl”). In some embodiments, a carbocyclyl group has 3 to 6 ring carbon atoms (“C3-6carbocyclyl”). In some embodiments, a carbocyclyl group has 4 to 6 ring carbon atoms (“C4-6 carbocyclyl”). In some embodiments, a carbocyclyl group has 5 to 6 ring carbon atoms (“C5-6 carbocyclyl”). In some embodiments, a carbocyclyl group has 5 to 10 ring carbon atoms (“C5-10carbocyclyl”). Exemplary C3-6carbocyclyl groups include cyclopropyl (C3), cyclopropenyl (C3), cyclobutyl (C4), cyclobutenyl (C4), cyclopentyl (C5), cyclopentenyl (C5), cyclohexyl (C6), cyclohexenyl (C6), cyclohexadienyl (C6), and the like. Exemplary C3-8 carbocyclyl groups include the aforementioned C3-6carbocyclyl groups as well as cycloheptyl (C7), cycloheptenyl (C7), cycloheptadienyl (C7), cycloheptatrienyl (C7), cyclooctyl (C8), cyclooctenyl (C8), bicyclo[2.2.1]heptanyl (C7), bicyclo[2.2.2]octanyl (C8), and the like. Exemplary C3-10 carbocyclyl groups include the aforementioned C3-8 carbocyclyl groups as well as cyclononyl (C9), cyclononenyl (C9), cyclodecyl (C10), cyclodecenyl (C10), octahydro-1H- indenyl (C9), decahydronaphthalenyl (C10), spiro[4.5]decanyl (C10), and the like. Exemplary C3-8 carbocyclyl groups include the aforementioned C3-10 carbocyclyl groups as well as cycloundecyl (C11), spiro[5.5]undecanyl (C11), cyclododecyl (C12), cyclododecenyl (C12), cyclotridecane (C13), cyclotetradecane (C14), and the like. As the foregoing examples illustrate, in certain embodiments, the carbocyclyl group is either monocyclic (“monocyclic carbocyclyl”) or polycyclic (e.g., containing a fused, bridged or spiro ring system such as a bicyclic system (“bicyclic carbocyclyl”) or tricyclic system (“tricyclic carbocyclyl”)) and can be saturated or can contain one or more carbon-carbon double or triple bonds. “Carbocyclyl” also includes ring systems wherein the carbocyclyl ring, as defined above, is fused with one or more aryl or #13447332v2 heteroaryl groups wherein the point of attachment is on the carbocyclyl ring, and in such instances, the number of carbons continue to designate the number of carbons in the carbocyclic ring system. Unless otherwise specified, each instance of a carbocyclyl group is independently unsubstituted (an “unsubstituted carbocyclyl”) or substituted (a “substituted carbocyclyl”) with one or more substituents. In certain embodiments, the carbocyclyl group is an unsubstituted C3-14 carbocyclyl. In certain embodiments, the carbocyclyl group is a substituted C3-14carbocyclyl. In some embodiments, “carbocyclyl” is a monocyclic, saturated carbocyclyl group having from 3 to 14 ring carbon atoms (“C3-14 cycloalkyl”). In some embodiments, a cycloalkyl group has 3 to 10 ring carbon atoms (“C3-10cycloalkyl”). In some embodiments, a cycloalkyl group has 3 to 8 ring carbon atoms (“C3-8 cycloalkyl”). In some embodiments, a cycloalkyl group has 3 to 6 ring carbon atoms (“C3-6 cycloalkyl”). In some embodiments, a cycloalkyl group has 4 to 6 ring carbon atoms (“C4-6cycloalkyl”). In some embodiments, a cycloalkyl group has 5 to 6 ring carbon atoms (“C5-6cycloalkyl”). In some embodiments, a cycloalkyl group has 5 to 10 ring carbon atoms (“C5-10 cycloalkyl”). Examples of C5-6 cycloalkyl groups include cyclopentyl (C5) and cyclohexyl (C5). Examples of C3-6 cycloalkyl groups include the aforementioned C5-6cycloalkyl groups as well as cyclopropyl (C3) and cyclobutyl (C4). Examples of C3-8 cycloalkyl groups include the aforementioned C3-6 cycloalkyl groups as well as cycloheptyl (C7) and cyclooctyl (C8). Unless otherwise specified, each instance of a cycloalkyl group is independently unsubstituted (an “unsubstituted cycloalkyl”) or substituted (a “substituted cycloalkyl”) with one or more substituents. In certain embodiments, the cycloalkyl group is an unsubstituted C3-14 cycloalkyl. In certain embodiments, the cycloalkyl group is a substituted C3-14cycloalkyl. In certain embodiments, the carbocyclyl includes 0, 1, or 2 C=C double bonds in the carbocyclic ring system, as valency permits. The term “heterocyclyl” or “heterocyclic” refers to a radical of a 3- to 14-membered non- aromatic ring system having ring carbon atoms and 1 to 4 ring heteroatoms, wherein each heteroatom is independently selected from nitrogen, oxygen, and sulfur (“3–14 membered heterocyclyl”). In heterocyclyl groups that contain one or more nitrogen atoms, the point of attachment can be a carbon or nitrogen atom, as valency permits. A heterocyclyl group can either be monocyclic (“monocyclic heterocyclyl”) or polycyclic (e.g., a fused, bridged or spiro ring system such as a bicyclic system (“bicyclic heterocyclyl”) or tricyclic system (“tricyclic heterocyclyl”)), and can be saturated or can contain one or more carbon-carbon double or triple bonds. Heterocyclyl polycyclic ring systems can include one or more heteroatoms in one or both rings. “Heterocyclyl” also includes ring systems wherein the heterocyclyl ring, as defined above, is fused with one or more carbocyclyl groups wherein the point of attachment is either on the carbocyclyl or heterocyclyl ring, or ring systems wherein the heterocyclyl ring, as defined #13447332v2 above, is fused with one or more aryl or heteroaryl groups, wherein the point of attachment is on the heterocyclyl ring, and in such instances, the number of ring members continue to designate the number of ring members in the heterocyclyl ring system. Unless otherwise specified, each instance of heterocyclyl is independently unsubstituted (an “unsubstituted heterocyclyl”) or substituted (a “substituted heterocyclyl”) with one or more substituents. In certain embodiments, the heterocyclyl group is an unsubstituted 3–14 membered heterocyclyl. In certain embodiments, the heterocyclyl group is a substituted 3–14 membered heterocyclyl. In certain embodiments, the heterocyclyl is substituted or unsubstituted, 3- to 7-membered, monocyclic heterocyclyl, wherein 1, 2, or 3 atoms in the heterocyclic ring system are independently oxygen, nitrogen, or sulfur, as valency permits. In some embodiments, a heterocyclyl group is a 5–10 membered non-aromatic ring system having ring carbon atoms and 1–4 ring heteroatoms, wherein each heteroatom is independently selected from nitrogen, oxygen, and sulfur (“5–10 membered heterocyclyl”). In some embodiments, a heterocyclyl group is a 5–8 membered non-aromatic ring system having ring carbon atoms and 1–4 ring heteroatoms, wherein each heteroatom is independently selected from nitrogen, oxygen, and sulfur (“5–8 membered heterocyclyl”). In some embodiments, a heterocyclyl group is a 5–6 membered non-aromatic ring system having ring carbon atoms and 1–4 ring heteroatoms, wherein each heteroatom is independently selected from nitrogen, oxygen, and sulfur (“5–6 membered heterocyclyl”). In some embodiments, the 5–6 membered heterocyclyl has 1–3 ring heteroatoms selected from nitrogen, oxygen, and sulfur. In some embodiments, the 5–6 membered heterocyclyl has 1–2 ring heteroatoms selected from nitrogen, oxygen, and sulfur. In some embodiments, the 5–6 membered heterocyclyl has 1 ring heteroatom selected from nitrogen, oxygen, and sulfur. Exemplary 3-membered heterocyclyl groups containing 1 heteroatom include azirdinyl, oxiranyl, and thiiranyl. Exemplary 4-membered heterocyclyl groups containing 1 heteroatom include azetidinyl, oxetanyl, and thietanyl. Exemplary 5-membered heterocyclyl groups containing 1 heteroatom include tetrahydrofuranyl, dihydrofuranyl, tetrahydrothiophenyl, dihydrothiophenyl, pyrrolidinyl, dihydropyrrolyl, and pyrrolyl-2,5-dione. Exemplary 5- membered heterocyclyl groups containing 2 heteroatoms include dioxolanyl, oxathiolanyl and dithiolanyl. Exemplary 5-membered heterocyclyl groups containing 3 heteroatoms include triazolinyl, oxadiazolinyl, and thiadiazolinyl. Exemplary 6-membered heterocyclyl groups containing 1 heteroatom include piperidinyl, tetrahydropyranyl, dihydropyridinyl, and thianyl. Exemplary 6-membered heterocyclyl groups containing 2 heteroatoms include piperazinyl, morpholinyl, dithianyl, and dioxanyl. Exemplary 6-membered heterocyclyl groups containing 3 heteroatoms include triazinyl. Exemplary 7-membered heterocyclyl groups containing 1 #13447332v2 heteroatom include azepanyl, oxepanyl, and thiepanyl. Exemplary 8-membered heterocyclyl groups containing 1 heteroatom include azocanyl, oxecanyl and thiocanyl. Exemplary bicyclic heterocyclyl groups include indolinyl, isoindolinyl, dihydrobenzofuranyl, dihydrobenzothienyl, tetrahydrobenzothienyl, tetrahydrobenzofuranyl, tetrahydroindolyl, tetrahydroquinolinyl, tetrahydroisoquinolinyl, decahydroquinolinyl, decahydroisoquinolinyl, octahydrochromenyl, octahydroisochromenyl, decahydronaphthyridinyl, decahydro-1,8-naphthyridinyl, octahydropyrrolo[3,2-b]pyrrole, indolinyl, phthalimidyl, naphthalimidyl, chromanyl, chromenyl, 1H-benzo[e][1,4]diazepinyl, 1,4,5,7-tetrahydropyrano[3,4-b]pyrrolyl, 5,6-dihydro-4H-furo[3,2- b]pyrrolyl, 6,7-dihydro-5H-furo[3,2-b]pyranyl, 5,7-dihydro-4H-thieno[2,3-c]pyranyl, 2,3- dihydro-1H-pyrrolo[2,3-b]pyridinyl, 2,3-dihydrofuro[2,3-b]pyridinyl, 4,5,6,7-tetrahydro-1H- pyrrolo[2,3-b]pyridinyl, 4,5,6,7-tetrahydrofuro[3,2-c]pyridinyl, 4,5,6,7-tetrahydrothieno[3,2- b]pyridinyl, 1,2,3,4-tetrahydro-1,6-naphthyridinyl, and the like. The term “aryl” refers to a radical of a monocyclic or polycyclic (e.g., bicyclic or tricyclic) 4n+2 aromatic ring system (e.g., having 6, 10, or 14 pi electrons shared in a cyclic array) having 6–14 ring carbon atoms and zero heteroatoms provided in the aromatic ring system (“C6-14aryl”). In some embodiments, an aryl group has 6 ring carbon atoms (“C6aryl”; e.g., phenyl). In some embodiments, an aryl group has 10 ring carbon atoms (“C10 aryl”; e.g., naphthyl such as 1–naphthyl and 2-naphthyl). In some embodiments, an aryl group has 14 ring carbon atoms (“C14aryl”; e.g., anthracyl). “Aryl” also includes ring systems wherein the aryl ring, as defined above, is fused with one or more carbocyclyl or heterocyclyl groups wherein the radical or point of attachment is on the aryl ring, and in such instances, the number of carbon atoms continue to designate the number of carbon atoms in the aryl ring system. Unless otherwise specified, each instance of an aryl group is independently unsubstituted (an “unsubstituted aryl”) or substituted (a “substituted aryl”) with one or more substituents. In certain embodiments, the aryl group is an unsubstituted C6-14 aryl. In certain embodiments, the aryl group is a substituted C6-14aryl. “Aralkyl” is a subset of “alkyl” and refers to an alkyl group substituted by an aryl group, wherein the point of attachment is on the alkyl moiety. The term “heteroaryl” refers to a radical of a 5-14 membered monocyclic or polycyclic (e.g., bicyclic, tricyclic) 4n+2 aromatic ring system (e.g., having 6, 10, or 14 ^ electrons shared in a cyclic array) having ring carbon atoms and 1–4 ring heteroatoms provided in the aromatic ring system, wherein each heteroatom is independently selected from nitrogen, oxygen, and sulfur (“5-14 membered heteroaryl”). In heteroaryl groups that contain one or more nitrogen atoms, the point of attachment can be a carbon or nitrogen atom, as valency permits. Heteroaryl polycyclic ring systems can include one or more heteroatoms in one or both rings. “Heteroaryl” #13447332v2 includes ring systems wherein the heteroaryl ring, as defined above, is fused with one or more carbocyclyl or heterocyclyl groups wherein the point of attachment is on the heteroaryl ring, and in such instances, the number of ring members continue to designate the number of ring members in the heteroaryl ring system. “Heteroaryl” also includes ring systems wherein the heteroaryl ring, as defined above, is fused with one or more aryl groups wherein the point of attachment is either on the aryl or heteroaryl ring, and in such instances, the number of ring members designates the number of ring members in the fused polycyclic (aryl / heteroaryl) ring system. Polycyclic heteroaryl groups wherein one ring does not contain a heteroatom (e.g., indolyl, quinolinyl, carbazolyl, and the like) the point of attachment can be on either ring, e.g., either the ring bearing a heteroatom (e.g., 2-indolyl) or the ring that does not contain a heteroatom (e.g., 5-indolyl). In certain embodiments, the heteroaryl is substituted or unsubstituted, 5- or 6-membered, monocyclic heteroaryl, wherein 1, 2, 3, or 4 atoms in the heteroaryl ring system are independently oxygen, nitrogen, or sulfur. In certain embodiments, the heteroaryl is substituted or unsubstituted, 9- or 10-membered, bicyclic heteroaryl, wherein 1, 2, 3, or 4 atoms in the heteroaryl ring system are independently oxygen, nitrogen, or sulfur. In some embodiments, a heteroaryl group is a 5-10 membered aromatic ring system having ring carbon atoms and 1–4 ring heteroatoms provided in the aromatic ring system, wherein each heteroatom is independently selected from nitrogen, oxygen, and sulfur (“5-10 membered heteroaryl”). In some embodiments, a heteroaryl group is a 5-8 membered aromatic ring system having ring carbon atoms and 1–4 ring heteroatoms provided in the aromatic ring system, wherein each heteroatom is independently selected from nitrogen, oxygen, and sulfur (“5-8 membered heteroaryl”). In some embodiments, a heteroaryl group is a 5-6 membered aromatic ring system having ring carbon atoms and 1–4 ring heteroatoms provided in the aromatic ring system, wherein each heteroatom is independently selected from nitrogen, oxygen, and sulfur (“5-6 membered heteroaryl”). In some embodiments, the 5-6 membered heteroaryl has 1–3 ring heteroatoms selected from nitrogen, oxygen, and sulfur. In some embodiments, the 5-6 membered heteroaryl has 1–2 ring heteroatoms selected from nitrogen, oxygen, and sulfur. In some embodiments, the 5-6 membered heteroaryl has 1 ring heteroatom selected from nitrogen, oxygen, and sulfur. Unless otherwise specified, each instance of a heteroaryl group is independently unsubstituted (an “unsubstituted heteroaryl”) or substituted (a “substituted heteroaryl”) with one or more substituents. In certain embodiments, the heteroaryl group is an unsubstituted 5-14 membered heteroaryl. In certain embodiments, the heteroaryl group is a substituted 5-14 membered heteroaryl. Exemplary 5-membered heteroaryl groups containing 1 heteroatom include pyrrolyl, furanyl, and thiophenyl. Exemplary 5-membered heteroaryl groups containing 2 heteroatoms #13447332v2 include imidazolyl, pyrazolyl, oxazolyl, isoxazolyl, thiazolyl, and isothiazolyl. Exemplary 5- membered heteroaryl groups containing 3 heteroatoms include triazolyl, oxadiazolyl, and thiadiazolyl. Exemplary 5-membered heteroaryl groups containing 4 heteroatoms include tetrazolyl. Exemplary 6-membered heteroaryl groups containing 1 heteroatom include pyridinyl. Exemplary 6-membered heteroaryl groups containing 2 heteroatoms include pyridazinyl, pyrimidinyl, and pyrazinyl. Exemplary 6-membered heteroaryl groups containing 3 or 4 heteroatoms include triazinyl and tetrazinyl, respectively. Exemplary 7-membered heteroaryl groups containing 1 heteroatom include azepinyl, oxepinyl, and thiepinyl. Exemplary 5,6- bicyclic heteroaryl groups include indolyl, isoindolyl, indazolyl, benzotriazolyl, benzothiophenyl, isobenzothiophenyl, benzofuranyl, benzoisofuranyl, benzimidazolyl, benzoxazolyl, benzisoxazolyl, benzoxadiazolyl, benzthiazolyl, benzisothiazolyl, benzthiadiazolyl, indolizinyl, and purinyl. Exemplary 6,6-bicyclic heteroaryl groups include naphthyridinyl, pteridinyl, quinolinyl, isoquinolinyl, cinnolinyl, quinoxalinyl, phthalazinyl, and quinazolinyl. Exemplary tricyclic heteroaryl groups include phenanthridinyl, dibenzofuranyl, carbazolyl, acridinyl, phenothiazinyl, phenoxazinyl, and phenazinyl. “Heteroaralkyl” is a subset of “alkyl” and refers to an alkyl group substituted by a heteroaryl group, wherein the point of attachment is on the alkyl moiety. The term “unsaturated bond” refers to a double or triple bond. The term “unsaturated” or “partially unsaturated” refers to a moiety that includes at least one double or triple bond. The term “saturated” or “fully saturated” refers to a moiety that does not contain a double or triple bond, e.g., the moiety only contains single bonds. Affixing the suffix “-ene” to a group indicates the group is a divalent moiety, e.g., alkylene is the divalent moiety of alkyl, alkenylene is the divalent moiety of alkenyl, alkynylene is the divalent moiety of alkynyl, heteroalkylene is the divalent moiety of heteroalkyl, heteroalkenylene is the divalent moiety of heteroalkenyl, heteroalkynylene is the divalent moiety of heteroalkynyl, carbocyclylene is the divalent moiety of carbocyclyl, heterocyclylene is the divalent moiety of heterocyclyl, arylene is the divalent moiety of aryl, and heteroarylene is the divalent moiety of heteroaryl. A group is optionally substituted unless expressly provided otherwise. The term “optionally substituted” refers to being substituted or unsubstituted. In certain embodiments, alkyl, alkenyl, alkynyl, heteroalkyl, heteroalkenyl, heteroalkynyl, carbocyclyl, heterocyclyl, aryl, and heteroaryl groups are optionally substituted. “Optionally substituted” refers to a group which is substituted or unsubstituted (e.g., “substituted” or “unsubstituted” alkyl, “substituted” or “unsubstituted” alkenyl, “substituted” or “unsubstituted” alkynyl, “substituted” or #13447332v2 “unsubstituted” heteroalkyl, “substituted” or “unsubstituted” heteroalkenyl, “substituted” or “unsubstituted” heteroalkynyl, “substituted” or “unsubstituted” carbocyclyl, “substituted” or “unsubstituted” heterocyclyl, “substituted” or “unsubstituted” aryl or “substituted” or “unsubstituted” heteroaryl group). In general, the term “substituted” means that at least one hydrogen present on a group is replaced with a permissible substituent, e.g., a substituent which upon substitution results in a stable compound, e.g., a compound which does not spontaneously undergo transformation such as by rearrangement, cyclization, elimination, or other reaction. Unless otherwise indicated, a “substituted” group has a substituent at one or more substitutable positions of the group, and when more than one position in any given structure is substituted, the substituent is either the same or different at each position. The term “substituted” is contemplated to include substitution with all permissible substituents of organic compounds, and includes any of the substituents described herein that results in the formation of a stable compound. The present disclosure contemplates any and all such combinations in order to arrive at a stable compound. For purposes of this disclosure, heteroatoms such as nitrogen may have hydrogen substituents and / or any suitable substituent as described herein which satisfy the valencies of the heteroatoms and results in the formation of a stable moiety. The disclosure is not limited in any manner by the exemplary substituents described herein. Exemplary carbon atom substituents include halogen, −CN, −NO2, −N3, −SO2H, −SO3H, −OH, −ORaa, −ON(Rbb)2, −N(Rbb)2, −N(Rbb)3+X−, −N(ORcc)Rbb, −SH, −SRaa, −SSRcc, −C(=O)Raa, −CO2H, −CHO, −C(ORcc)2, −CO2Raa, −OC(=O)Raa, −OCO2Raa, −C(=O)N(Rbb)2, −P(ORcc)2, −P(Rcc)3+X−, −P(ORcc)3+X−, −P(Rcc)4, −P(ORcc)4, −OP(Rcc)2, −OP(Rcc)3+X−, −OP(ORcc)2, −OP(ORcc)3+X−, −OP(Rcc)4, −OP(ORcc)4, −B(Raa)2, −B(ORcc)2, −BRaa(ORcc), C1–20alkyl, C1–20 perhaloalkyl, C1–20 alkenyl, C1–20 alkynyl, heteroC1–20 alkyl, heteroC1–20 alkenyl, heteroC1–20 alkynyl, C3-10 carbocyclyl, 3-14 membered heterocyclyl, C6-14 aryl, and 5-14 membered heteroaryl, wherein each alkyl, alkenyl, alkynyl, heteroalkyl, heteroalkenyl, heteroalkynyl, carbocyclyl, heterocyclyl, aryl, and heteroaryl is independently substituted with 0, 1, 2, 3, 4, or 5 Rddgroups; wherein X−is a counterion; #13447332v2 or two geminal hydrogens on a carbon atom are replaced with the group =O, =S, =NN(Rbb)2, =NNRbbC(=O)Raa, =NNRbbC(=O)ORaa, =NNRbbS(=O)2Raa, =NRbb, or =NORcc; wherein: each instance of Raais, independently, selected from C1–20 alkyl, C1–20 perhaloalkyl, C1–20 alkenyl, C1–20 alkynyl, heteroC1–20 alkyl, heteroC1–20alkenyl, heteroC1–20alkynyl, C3-10 carbocyclyl, 3-14 membered heterocyclyl, C6-14aryl, and 5-14 membered heteroaryl, or two Raagroups are joined to form a 3-14 membered heterocyclyl or 5-14 membered heteroaryl ring, wherein each of the alkyl, alkenyl, alkynyl, heteroalkyl, heteroalkenyl, heteroalkynyl, carbocyclyl, heterocyclyl, aryl, and heteroaryl is independently substituted with 0, 1, 2, 3, 4, or 5 Rddgroups; each instance of Rbbis, independently, selected from hydrogen, −OH, −ORaa, −N(Rcc)2, −CN, −C(=O)Raa, −C(=O)N(Rcc)2, −CO2Raa, −SO2Raa, −C(=NRcc)ORaa, −C(=NRcc)N(Rcc)2, −SO2N(Rcc)2, −SO2Rcc, −SO2ORcc, −SORaa, −C(=S)N(Rcc)2, −C(=O)SRcc, −C(=S)SRcc, −P(=O)(Raa)2, −P(=O)(ORcc)2, −P(=O)(N(Rcc)2)2, C1–20 alkyl, C1–20 perhaloalkyl, C1–20 alkenyl, C1–20 alkynyl, heteroC1–20alkyl, heteroC1–20alkenyl, heteroC1–20alkynyl, C3-10 carbocyclyl, 3-14 membered heterocyclyl, C6-14aryl, and 5-14 membered heteroaryl, or two Rbbgroups are joined to form a 3-14 membered heterocyclyl or 5-14 membered heteroaryl ring, wherein each alkyl, alkenyl, alkynyl, heteroalkyl, heteroalkenyl, heteroalkynyl, carbocyclyl, heterocyclyl, aryl, and heteroaryl is independently substituted with 0, 1, 2, 3, 4, or 5 Rddgroups; each instance of Rccis, independently, selected from hydrogen, C1–20 alkyl, C1–20 perhaloalkyl, C1–20 alkenyl, C1–20 alkynyl, heteroC1–20 alkyl, heteroC1–20 alkenyl, heteroC1–20 alkynyl, C3-10carbocyclyl, 3-14 membered heterocyclyl, C6-14aryl, and 5-14 membered heteroaryl, or two Rccgroups are joined to form a 3-14 membered heterocyclyl or 5-14 membered heteroaryl ring, wherein each alkyl, alkenyl, alkynyl, heteroalkyl, heteroalkenyl, heteroalkynyl, carbocyclyl, heterocyclyl, aryl, and heteroaryl is independently substituted with 0, 1, 2, 3, 4, or 5 Rddgroups; each instance of Rddis, independently, selected from halogen, −CN, −NO2, −N3, −SO2H, −SO3H, −OH, −ORee, −ON(Rff)2, −N(Rff)2, −N(Rff)3+X−, −N(ORee)Rff, −SH, −SRee, −SSRee, −C(=O)Ree, −CO2H, −CO2Ree, −OC(=O)Ree, −OCO2Ree, −C(=O)N(Rff)2, −OC(=O)N(Rff)2, −OC(=NRff)ORee, −C(=NRff)N(Rff)2, −OC(=NRff)N(Rff)2, −NRffC(=NRff)N(Rff)2, −NRffSO2Ree, −SO2N(Rff)2, −SO2Ree, −SO2ORee, −OSO2Ree, −S(=O)Ree, −Si(Ree)3, −OSi(Ree)3, −C(=S)N(Rff)2, −C(=O)SRee, −C(=S)SRee, −SC(=S)SRee, −P(=O)(ORee)2, −P(=O)(Ree)2, −OP(=O)(Ree)2, −OP(=O)(ORee)2, C1–10 alkyl, C1–10 perhaloalkyl, C1–10 alkenyl, C1–10 alkynyl, heteroC1–10alkyl, heteroC1–10alkenyl, heteroC1–10alkynyl, C3-10 carbocyclyl, 3-10 membered heterocyclyl, C6-10 #13447332v2 aryl, and 5-10 membered heteroaryl, wherein each alkyl, alkenyl, alkynyl, heteroalkyl, heteroalkenyl, heteroalkynyl, carbocyclyl, heterocyclyl, aryl, and heteroaryl is independently substituted with 0, 1, 2, 3, 4, or 5 Rgggroups, or two geminal Rddsubstituents are joined to form =O or =S; wherein X−is a counterion; each instance of Reeis, independently, selected from C1–10 alkyl, C1–10 perhaloalkyl, C1–10 alkenyl, C1–10alkynyl, heteroC1–10alkyl, heteroC1–10alkenyl, heteroC1–10alkynyl, C3-10carbocyclyl, C6-10 aryl, 3-10 membered heterocyclyl, and 3-10 membered heteroaryl, wherein each alkyl, alkenyl, alkynyl, heteroalkyl, heteroalkenyl, heteroalkynyl, carbocyclyl, heterocyclyl, aryl, and heteroaryl is independently substituted with 0, 1, 2, 3, 4, or 5 Rgggroups; each instance of Rffis, independently, selected from hydrogen, C1–10 alkyl, C1–10 perhaloalkyl, C1–10 alkenyl, C1–10 alkynyl, heteroC1–10 alkyl, heteroC1–10 alkenyl, heteroC1–10 alkynyl, C3-10carbocyclyl, 3-10 membered heterocyclyl, C6-10aryl, and 5-10 membered heteroaryl, or two Rffgroups are joined to form a 3-10 membered heterocyclyl or 5-10 membered heteroaryl ring, wherein each alkyl, alkenyl, alkynyl, heteroalkyl, heteroalkenyl, heteroalkynyl, carbocyclyl, heterocyclyl, aryl, and heteroaryl is independently substituted with 0, 1, 2, 3, 4, or 5 Rgggroups; each instance of Rggis, independently, halogen, −CN, −NO2, −N3, −SO2H, −SO3H, −OH, −OC1–6 alkyl, −ON(C1–6 alkyl)2, −N(C1–6 alkyl)2, −N(C1–6 alkyl)3+X−, −NH(C1–6 alkyl)2+X−, −NH2(C1–6alkyl)+X−, −NH3+X−, −N(OC1–6alkyl)(C1–6alkyl), −N(OH)(C1–6alkyl), −NH(OH), −SH, −SC1–6 alkyl, −SS(C1–6 alkyl), −C(=O)(C1–6 alkyl), −CO2H, −CO2(C1–6 alkyl), −OC(=O)(C1–6 alkyl), −OCO2(C1–6 alkyl), −C(=O)NH2, −C(=O)N(C1–6 alkyl)2, −OC(=O)NH(C1–6alkyl), −NHC(=O)( C1–6alkyl), −N(C1–6alkyl)C(=O)( C1–6alkyl), −NHCO2(C1–6alkyl), −NHC(=O)N(C1–6alkyl)2, −NHC(=O)NH(C1–6alkyl), −NHC(=O)NH2, −C(=NH)O(C1–6 alkyl), −OC(=NH)(C1–6 alkyl), −OC(=NH)OC1–6 alkyl, −C(=NH)N(C1–6 alkyl)2, −C(=NH)NH(C1–6 alkyl), −C(=NH)NH2, −OC(=NH)N(C1–6 alkyl)2, −OC(NH)NH(C1–6 alkyl), −OC(NH)NH2, −NHC(NH)N(C1–6alkyl)2, −NHC(=NH)NH2, −NHSO2(C1–6alkyl), −SO2N(C1–6 alkyl)2, −SO2NH(C1–6 alkyl), −SO2NH2, −SO2C1–6 alkyl, −SO2OC1–6 alkyl, −OSO2C1–6 alkyl, −SOC1–6 alkyl, −Si(C1–6 alkyl)3, −OSi(C1–6 alkyl)3 −C(=S)N(C1–6 alkyl)2, C(=S)NH(C1–6alkyl), C(=S)NH2, −C(=O)S(C1–6alkyl), −C(=S)SC1–6alkyl, −SC(=S)SC1–6alkyl, −P(=O)(OC1–6 alkyl)2, −P(=O)(C1–6 alkyl)2, −OP(=O)(C1–6 alkyl)2, −OP(=O)(OC1–6 alkyl)2, C1– 10 alkyl, C1–10 perhaloalkyl, C1–10 alkenyl, C1–10 alkynyl, heteroC1–10 alkyl, heteroC1–10 alkenyl, heteroC1–10alkynyl, C3-10carbocyclyl, C6-10aryl, 3-10 membered heterocyclyl, or 5-10 membered heteroaryl; or two geminal Rggsubstituents can be joined to form =O or =S; and each X−is a counterion. #13447332v2 In certain embodiments, each carbon atom substituent is independently halogen, substituted (e.g., substituted with one or more halogen) or unsubstituted C1-6alkyl, −ORaa, −SRaa, −N(Rbb)2, –CN, –SCN, –NO2, −C(=O)Raa, −CO2Raa, −C(=O)N(Rbb)2, −OC(=O)Raa, certain embodiments, each carbon atom substituent is independently halogen, substituted (e.g., substituted with one or more halogen) or unsubstituted C1–10alkyl, −ORaa, −SRaa, −N(Rbb)2, –CN, –SCN, –NO2, −C(=O)Raa, −CO2Raa, −C(=O)N(Rbb)2, −OC(=O)Raa, −OCO2Raa, Raais hydrogen, substituted (e.g., substituted with one or more halogen) or unsubstituted C1–10alkyl, an oxygen protecting group (e.g., silyl, TBDPS, TBDMS, TIPS, TES, TMS, MOM, THP, t-Bu, Bn, allyl, acetyl, pivaloyl, or benzoyl) when attached to an oxygen atom, or a sulfur protecting group (e.g., acetamidomethyl, t-Bu, 3-nitro-2-pyridine sulfenyl, 2-pyridine-sulfenyl, or triphenylmethyl) when attached to a sulfur atom; and each Rbbis independently hydrogen, substituted (e.g., substituted with one or more halogen) or unsubstituted C1–10 alkyl, or a nitrogen protecting group (e.g., Bn, Boc, Cbz, Fmoc, trifluoroacetyl, triphenylmethyl, acetyl, or Ts). In certain embodiments, each carbon atom substituent is independently halogen, substituted (e.g., substituted with one or more halogen) or unsubstituted C1-6 alkyl, −ORaa, −SRaa, −N(Rbb)2, –CN, –SCN, or –NO2. In certain embodiments, each carbon atom substituent is independently halogen, substituted (e.g., substituted with one or more halogen moieties) or unsubstituted C1–10alkyl, −ORaa, −SRaa, −N(Rbb)2, –CN, –SCN, or –NO2, wherein Raais hydrogen, substituted (e.g., substituted with one or more halogen) or unsubstituted C1–10 alkyl, an oxygen protecting group (e.g., silyl, TBDPS, TBDMS, TIPS, TES, TMS, MOM, THP, t-Bu, Bn, allyl, acetyl, pivaloyl, or benzoyl) when attached to an oxygen atom, or a sulfur protecting group (e.g., acetamidomethyl, t-Bu, 3-nitro-2-pyridine sulfenyl, 2-pyridine-sulfenyl, or triphenylmethyl) when attached to a sulfur atom; and each Rbbis independently hydrogen, substituted (e.g., substituted with one or more halogen) or unsubstituted C1–10alkyl, or a nitrogen protecting group (e.g., Bn, Boc, Cbz, Fmoc, trifluoroacetyl, triphenylmethyl, acetyl, or Ts). In certain embodiments, the molecular weight of a carbon atom substituent is lower than 250, lower than 200, lower than 150, lower than 100, or lower than 50 g / mol. In certain embodiments, a carbon atom substituent consists of carbon, hydrogen, fluorine, chlorine, bromine, iodine, oxygen, sulfur, nitrogen, and / or silicon atoms. In certain embodiments, a carbon atom substituent consists of carbon, hydrogen, fluorine, chlorine, bromine, iodine, oxygen, sulfur, and / or nitrogen atoms. In certain embodiments, a carbon atom substituent consists of carbon, hydrogen, fluorine, chlorine, bromine, and / or iodine atoms. In certain #13447332v2 embodiments, a carbon atom substituent consists of carbon, hydrogen, fluorine, and / or chlorine atoms. The term “halo” or “halogen” refers to fluorine (fluoro, −F), chlorine (chloro, −Cl), bromine (bromo, −Br), or iodine (iodo, −I). The term “hydroxyl” or “hydroxy” refers to the group −OH. The term “substituted hydroxyl” or “substituted hydroxyl,” by extension, refers to a hydroxyl group wherein the oxygen atom directly attached to the parent molecule is substituted with a group other than hydrogen, and includes groups selected from −ORaa, −ON(Rbb)2, −OC(=O)SRaa, −OC(=O)Raa, −OCO2Raa, −OC(=O)N(Rbb)2, −OC(=NRbb)Raa, −OC(=NRbb)ORaa, −OC(=NRbb)N(Rbb)2, −OS(=O)Raa, −OSO2Raa, −OSi(Raa)3, −OP(Rcc)2, −OP(Rcc)3+X−, −OP(ORcc)2, −OP(ORcc)3+X−, −OP(=O)(Raa)2, −OP(=O)(ORcc)2, and −OP(=O)(N(Rbb))2, wherein X−, Raa, Rbb, and Rccare as defined herein. The term “thiol” or “thio” refers to the group –SH. The term “substituted thiol” or “substituted thio,” by extension, refers to a thiol group wherein the sulfur atom directly attached to the parent molecule is substituted with a group other than hydrogen, and includes groups selected from –SRaa, –S=SRcc, –SC(=S)SRaa, –SC(=S)ORaa, –SC(=S) N(Rbb)2, –SC(=O)SRaa, –SC(=O)ORaa, –SC(=O)N(Rbb)2, and –SC(=O)Raa, wherein Raaand Rccare as defined herein. The term “amino” refers to the group −NH2. The term “substituted amino,” by extension, refers to a monosubstituted amino, a disubstituted amino, or a trisubstituted amino. In certain embodiments, the “substituted amino” is a monosubstituted amino or a disubstituted amino group. The term “monosubstituted amino” refers to an amino group wherein the nitrogen atom directly attached to the parent molecule is substituted with one hydrogen and one group other than hydrogen, and includes groups selected from −NH(Rbb), −NHC(=O)Raa, −NHCO2Raa, −NHC(=O)N(Rbb)2, −NHC(=NRbb)N(Rbb)2, −NHSO2Raa, −NHP(=O)(ORcc)2, and −NHP(=O)(N(Rbb)2)2, wherein Raa, Rbband Rccare as defined herein, and wherein Rbbof the group −NH(Rbb) is not hydrogen. The term “disubstituted amino” refers to an amino group wherein the nitrogen atom directly attached to the parent molecule is substituted with two groups other than hydrogen, and includes groups selected from −N(Rbb)2, −NRbbC(=O)Raa, −NRbbCO2Raa, −NRbbC(=O)N(Rbb)2, −NRbbC(=NRbb)N(Rbb)2, −NRbbSO2Raa, −NRbbP(=O)(ORcc)2, and −NRbbP(=O)(N(Rbb)2)2, wherein Raa, Rbb, and Rccare as defined herein, with the proviso that the nitrogen atom directly attached to the parent molecule is not substituted with hydrogen. #13447332v2 The term “trisubstituted amino” refers to an amino group wherein the nitrogen atom directly attached to the parent molecule is substituted with three groups, and includes groups selected from −N(Rbb)3and −N(Rbb)3+X−, wherein Rbband X−are as defined herein. The term “acyl” refers to a group having the general formula −C(=O)RX1, −C(=O)ORX1, −C(=O)−O−C(=O)RX1, −C(=O)SRX1, −C(=O)N(RX1)2, −C(=S)RX1, −C(=S)N(RX1)2, and −C(=S)S(RX1), −C(=NRX1)RX1, −C(=NRX1)ORX1, −C(=NRX1)SRX1, and −C(=NRX1)N(RX1)2, wherein RX1is hydrogen; halogen; substituted or unsubstituted hydroxyl; substituted or unsubstituted thiol; substituted or unsubstituted amino; substituted or unsubstituted acyl, cyclic or acyclic, substituted or unsubstituted, branched or unbranched aliphatic; cyclic or acyclic, substituted or unsubstituted, branched or unbranched heteroaliphatic; cyclic or acyclic, substituted or unsubstituted, branched or unbranched alkyl; cyclic or acyclic, substituted or unsubstituted, branched or unbranched alkenyl; substituted or unsubstituted alkynyl; substituted or unsubstituted aryl, substituted or unsubstituted heteroaryl, aliphaticoxy, heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy, heteroarylthioxy, mono- or di- aliphaticamino, mono- or di- heteroaliphaticamino, mono- or di- alkylamino, mono- or di- heteroalkylamino, mono- or di-arylamino, or mono- or di-heteroarylamino; or two RX1groups taken together form a 5- to 6-membered heterocyclic ring. Exemplary acyl groups include aldehydes (−CHO), carboxylic acids (−CO2H), ketones, acyl halides, esters, amides, imines, carbonates, carbamates, and ureas. Acyl substituents include, but are not limited to, any of the substituents described herein, that result in the formation of a stable moiety (e.g., aliphatic, alkyl, alkenyl, alkynyl, heteroaliphatic, heterocyclic, aryl, heteroaryl, acyl, oxo, imino, thiooxo, cyano, isocyano, amino, azido, nitro, hydroxyl, thiol, halo, aliphaticamino, heteroaliphaticamino, alkylamino, heteroalkylamino, arylamino, heteroarylamino, alkylaryl, arylalkyl, aliphaticoxy, heteroaliphaticoxy, alkyloxy, heteroalkyloxy, aryloxy, heteroaryloxy, aliphaticthioxy, heteroaliphaticthioxy, alkylthioxy, heteroalkylthioxy, arylthioxy, heteroarylthioxy, acyloxy, and the like, each of which may or may not be further substituted). The term “carbonyl” refers to a group wherein the carbon directly attached to the parent molecule is sp2hybridized, and is substituted with an oxygen, nitrogen or sulfur atom, e.g., a group selected from ketones (–C(=O)Raa), carboxylic acids (–CO2H), aldehydes (–CHO), esters (–CO2Raa, –C(=O)SRaa, –C(=S)SRaa), amides (–C(=O)N(Rbb)2, –C(=O)NRbbSO2Raa, −C(=S)N(Rbb)2), and imines (–C(=NRbb)Raa, –C(=NRbb)ORaa), –C(=NRbb)N(Rbb)2), wherein Raaand Rbbare as defined herein. The term “silyl” refers to the group –Si(Raa)3, wherein Raais as defined herein. The term “oxo” refers to the group =O, and the term “thiooxo” refers to the group =S. #13447332v2 Nitrogen atoms can be substituted or unsubstituted as valency permits, and include primary, secondary, tertiary, and quaternary nitrogen atoms. Exemplary nitrogen atom substituents include hydrogen, −OH, −ORaa, −N(Rcc)2, −CN, −C(=O)Raa, −C(=O)N(Rcc)2, −CO2Raa, −SO2Raa, −C(=NRbb)Raa, −C(=NRcc)ORaa, −C(=NRcc)N(Rcc)2, −SO2N(Rcc)2, −SO2Rcc, −P(=O)(N(Rcc)2)2, C1–20alkyl, C1–20perhaloalkyl, C1–20alkenyl, C1–20alkynyl, hetero C1–20alkyl, hetero C1–20 alkenyl, hetero C1–20 alkynyl, C3-10 carbocyclyl, 3-14 membered heterocyclyl, C6-14 aryl, and 5-14 membered heteroaryl, or two Rccgroups attached to an N atom are joined to form a 3-14 membered heterocyclyl or 5-14 membered heteroaryl ring, wherein each alkyl, alkenyl, alkynyl, heteroalkyl, heteroalkenyl, heteroalkynyl, carbocyclyl, heterocyclyl, aryl, and heteroaryl is independently substituted with 0, 1, 2, 3, 4, or 5 Rddgroups, and wherein Raa, Rbb, Rccand Rddare as defined above. In certain embodiments, each nitrogen atom substituent is independently substituted (e.g., substituted with one or more halogen) or unsubstituted C1-6 alkyl, −C(=O)Raa, −CO2Raa, −C(=O)N(Rbb)2, or a nitrogen protecting group. In certain embodiments, each nitrogen atom substituent is independently substituted (e.g., substituted with one or more halogen) or unsubstituted C1-10 alkyl, −C(=O)Raa, −CO2Raa, −C(=O)N(Rbb)2, or a nitrogen protecting group, wherein Raais hydrogen, substituted (e.g., substituted with one or more halogen) or unsubstituted C1-10alkyl, or an oxygen protecting group when attached to an oxygen atom; and each Rbbis independently hydrogen, substituted (e.g., substituted with one or more halogen) or unsubstituted C1-10 alkyl, or a nitrogen protecting group. In certain embodiments, each nitrogen atom substituent is independently substituted (e.g., substituted with one or more halogen) or unsubstituted C1-6alkyl or a nitrogen protecting group. In certain embodiments, the substituent present on the nitrogen atom is a nitrogen protecting group (also referred to herein as an “amino protecting group”). Nitrogen protecting groups include −OH, −ORaa, −N(Rcc)2, −C(=O)Raa, −C(=O)N(Rcc)2, −CO2Raa, −SO2Raa, −C(=NRcc)Raa, −C(=NRcc)ORaa, −C(=NRcc)N(Rcc)2, −SO2N(Rcc)2, −SO2Rcc, −SO2ORcc, −SORaa, −C(=S)N(Rcc)2, −C(=O)SRcc, −C(=S)SRcc, C1–10 alkyl (e.g., aralkyl, heteroaralkyl), C1–20 alkenyl, C1–20alkynyl, hetero C1–20alkyl, hetero C1–20alkenyl, hetero C1–20alkynyl, C3-10carbocyclyl, 3-14 membered heterocyclyl, C6-14 aryl, and 5-14 membered heteroaryl groups, wherein each alkyl, alkenyl, alkynyl, heteroalkyl, heteroalkenyl, heteroalkynyl, carbocyclyl, heterocyclyl, aralkyl, aryl, and heteroaryl is independently substituted with 0, 1, 2, 3, 4, or 5 Rddgroups, and wherein Raa, Rbb, Rccand Rddare as defined herein. Nitrogen protecting groups are well known in the art and include those described in detail in Protecting Groups in Organic #13447332v2 Synthesis, T. W. Greene and P. G. M. Wuts, 3rdedition, John Wiley & Sons, 1999, incorporated herein by reference. For example, in certain embodiments, at least one nitrogen protecting group is an amide group (e.g., a moiety that include the nitrogen atom to which the nitrogen protecting groups (e.g., −C(=O)Raa) is directly attached). In certain such embodiments, each nitrogen protecting group, together with the nitrogen atom to which the nitrogen protecting group is attached, is independently selected from the group consisting of formamide, acetamide, chloroacetamide, trichloroacetamide, trifluoroacetamide, phenylacetamide, 3-phenylpropanamide, picolinamide, 3-pyridylcarboxamide, N-benzoylphenylalanyl derivatives, benzamide, p-phenylbenzamide, o- nitophenylacetamide, o-nitrophenoxyacetamide, acetoacetamide, (N’- dithiobenzyloxyacylamino)acetamide, 3-(p-hydroxyphenyl)propanamide, 3-(o- nitrophenyl)propanamide, 2-methyl-2-(o-nitrophenoxy)propanamide, 2-methyl-2-(o- phenylazophenoxy)propanamide, 4-chlorobutanamide, 3-methyl-3-nitrobutanamide, o- nitrocinnamide, N-acetylmethionine derivatives, o-nitrobenzamide, and o- (benzoyloxymethyl)benzamide. In certain embodiments, at least one nitrogen protecting group is a carbamate group (e.g., a moiety that include the nitrogen atom to which the nitrogen protecting groups (e.g., −C(=O)ORaa) is directly attached). In certain such embodiments, each nitrogen protecting group, together with the nitrogen atom to which the nitrogen protecting group is attached, is independently selected from the group consisting of methyl carbamate, ethyl carbamate, 9- fluorenylmethyl carbamate (Fmoc), 9-(2-sulfo)fluorenylmethyl carbamate, 9-(2,7- dibromo)fluoroenylmethyl carbamate, 2,7-di-t-butyl-[9-(10,10-dioxo-10,10,10,10- tetrahydrothioxanthyl)]methyl carbamate (DBD-Tmoc), 4-methoxyphenacyl carbamate (Phenoc), 2,2,2-trichloroethyl carbamate (Troc), 2-trimethylsilylethyl carbamate (Teoc), 2- phenylethyl carbamate (hZ), 1–(1-adamantyl)-1-methylethyl carbamate (Adpoc), 1,1-dimethyl- 2-haloethyl carbamate, 1,1-dimethyl-2,2-dibromoethyl carbamate (DB-t-BOC), 1,1-dimethyl- 2,2,2-trichloroethyl carbamate (TCBOC), 1-methyl-1-(4-biphenylyl)ethyl carbamate (Bpoc), 1- (3,5-di-t-butylphenyl)-1-methylethyl carbamate (t-Bumeoc), 2-(2′- and 4′-pyridyl)ethyl carbamate (Pyoc), 2-(N,N-dicyclohexylcarboxamido)ethyl carbamate, t-butyl carbamate (BOC or Boc), 1-adamantyl carbamate (Adoc), vinyl carbamate (Voc), allyl carbamate (Alloc), 1- isopropylallyl carbamate (Ipaoc), cinnamyl carbamate (Coc), 4-nitrocinnamyl carbamate (Noc), 8-quinolyl carbamate, N-hydroxypiperidinyl carbamate, alkyldithio carbamate, benzyl carbamate (Cbz), p-methoxybenzyl carbamate (Moz), p-nitobenzyl carbamate, p-bromobenzyl carbamate, p-chlorobenzyl carbamate, 2,4-dichlorobenzyl carbamate, 4-methylsulfinylbenzyl carbamate (Msz), 9-anthrylmethyl carbamate, diphenylmethyl carbamate, 2-methylthioethyl #13447332v2 carbamate, 2-methylsulfonylethyl carbamate, 2-(p-toluenesulfonyl)ethyl carbamate, [2-(1,3- dithianyl)]methyl carbamate (Dmoc), 4-methylthiophenyl carbamate (Mtpc), 2,4- dimethylthiophenyl carbamate (Bmpc), 2-phosphonioethyl carbamate (Peoc), 2- triphenylphosphonioisopropyl carbamate (Ppoc), 1,1-dimethyl-2-cyanoethyl carbamate, m- chloro-p-acyloxybenzyl carbamate, p-(dihydroxyboryl)benzyl carbamate, 5- benzisoxazolylmethyl carbamate, 2-(trifluoromethyl)-6-chromonylmethyl carbamate (Tcroc), m- nitrophenyl carbamate, 3,5-dimethoxybenzyl carbamate, o-nitrobenzyl carbamate, 3,4- dimethoxy-6-nitrobenzyl carbamate, phenyl(o-nitrophenyl)methyl carbamate, t-amyl carbamate, S-benzyl thiocarbamate, p-cyanobenzyl carbamate, cyclobutyl carbamate, cyclohexyl carbamate, cyclopentyl carbamate, cyclopropylmethyl carbamate, p-decyloxybenzyl carbamate, 2,2- dimethoxyacylvinyl carbamate, o-(N,N-dimethylcarboxamido)benzyl carbamate, 1,1-dimethyl- 3-(N,N-dimethylcarboxamido)propyl carbamate, 1,1-dimethylpropynyl carbamate, di(2- pyridyl)methyl carbamate, 2-furanylmethyl carbamate, 2-iodoethyl carbamate, isoborynl carbamate, isobutyl carbamate, isonicotinyl carbamate, p-(p’-methoxyphenylazo)benzyl carbamate, 1-methylcyclobutyl carbamate, 1-methylcyclohexyl carbamate, 1-methyl-1- cyclopropylmethyl carbamate, 1-methyl-1-(3,5-dimethoxyphenyl)ethyl carbamate, 1-methyl-1- (p-phenylazophenyl)ethyl carbamate, 1-methyl-1-phenylethyl carbamate, 1-methyl-1-(4- pyridyl)ethyl carbamate, phenyl carbamate, p-(phenylazo)benzyl carbamate, 2,4,6-tri-t- butylphenyl carbamate, 4-(trimethylammonium)benzyl carbamate, and 2,4,6- carbamate. In certain embodiments, at least one nitrogen protecting group is a sulfonamide group (e.g., a moiety that include the nitrogen atom to which the nitrogen protecting groups (e.g., −S(=O)2Raa) is directly attached). In certain such embodiments, each nitrogen protecting group, together with the nitrogen atom to which the nitrogen protecting group is attached, is independently selected from the group consisting of p-toluenesulfonamide (Ts), benzenesulfonamide, 2,3,6-trimethyl-4-methoxybenzenesulfonamide (Mtr), 2,4,6- trimethoxybenzenesulfonamide (Mtb), 2,6-dimethyl-4-methoxybenzenesulfonamide (Pme), 2,3,5,6-tetramethyl-4-methoxybenzenesulfonamide (Mte), 4-methoxybenzenesulfonamide (Mbs), 2,4,6-trimethylbenzenesulfonamide (Mts), 2,6-dimethoxy-4-methylbenzenesulfonamide (iMds), 2,2,5,7,8-pentamethylchroman-6-sulfonamide (Pmc), methanesulfonamide (Ms), β- trimethylsilylethanesulfonamide (SES), 9-anthracenesulfonamide, 4-(4′,8′- dimethoxynaphthylmethyl)benzenesulfonamide (DNMBS), benzylsulfonamide, trifluoromethylsulfonamide, and phenacylsulfonamide. In certain embodiments, each nitrogen protecting group, together with the nitrogen atom to which the nitrogen protecting group is attached, is independently selected from the group #13447332v2 consisting of phenothiazinyl-(10)-acyl derivatives, N’-p-toluenesulfonylaminoacyl derivatives, N’-phenylaminothioacyl derivatives, N-benzoylphenylalanyl derivatives, N-acetylmethionine derivatives, 4,5-diphenyl-3-oxazolin-2-one, N-phthalimide, N-dithiasuccinimide (Dts), N-2,3- diphenylmaleimide, N-2,5-dimethylpyrrole, N-1,1,4,4-tetramethyldisilylazacyclopentane adduct (STABASE), 5-substituted 1,3-dimethyl-1,3,5-triazacyclohexan-2-one, 5-substituted 1,3- dibenzyl-1,3,5-triazacyclohexan-2-one, 1-substituted 3,5-dinitro-4-pyridone, N-methylamine, N- allylamine, N-[2-(trimethylsilyl)ethoxy]methylamine (SEM), N-3-acetoxypropylamine, N-(1- isopropyl-4-nitro-2-oxo-3-pyroolin-3-yl)amine, quaternary ammonium salts, N-benzylamine, N- di(4-methoxyphenyl)methylamine, N-5-dibenzosuberylamine, N-triphenylmethylamine (Tr), N- [(4-methoxyphenyl)diphenylmethyl]amine (MMTr), N-9-phenylfluorenylamine (PhF), N-2,7- dichloro-9-fluorenylmethyleneamine, N-ferrocenylmethylamino (Fcm), N-2-picolylamino N’- oxide, N-1,1-dimethylthiomethyleneamine, N-benzylideneamine, N-p- methoxybenzylideneamine, N-diphenylmethyleneamine, N-[(2-pyridyl)mesityl]methyleneamine, N-(N’,N’-dimethylaminomethylene)amine, N-p-nitrobenzylideneamine, N-salicylideneamine, N- 5-chlorosalicylideneamine, N-(5-chloro-2-hydroxyphenyl)phenylmethyleneamine, N- cyclohexylideneamine, N-(5,5-dimethyl-3-oxo-1-cyclohexenyl)amine, N-borane derivatives, N- diphenylborinic acid derivatives, N-[phenyl(pentaacylchromium- or tungsten)acyl]amine, N- copper chelate, N-zinc chelate, N-nitroamine, N-nitrosoamine, amine N-oxide, diphenylphosphinamide (Dpp), dimethylthiophosphinamide (Mpt), diphenylthiophosphinamide (Ppt), dialkyl phosphoramidates, dibenzyl phosphoramidate, diphenyl phosphoramidate, benzenesulfenamide, o-nitrobenzenesulfenamide (Nps), 2,4-dinitrobenzenesulfenamide, pentachlorobenzenesulfenamide, 2-nitro-4-methoxybenzenesulfenamide, triphenylmethylsulfenamide, and 3-nitropyridinesulfenamide (Npys). In some embodiments, two instances of a nitrogen protecting group together with the nitrogen atoms to which the nitrogen protecting groups are attached are N,N’-isopropylidenediamine. In certain embodiments, at least one nitrogen protecting group is Bn, Boc, Cbz, Fmoc, trifluoroacetyl, triphenylmethyl, acetyl, or Ts. In certain embodiments, each oxygen atom substituent is independently substituted (e.g., substituted with one or more halogen) or unsubstituted C1-10alkyl, −C(=O)Raa, −CO2Raa, −C(=O)N(Rbb)2, or an oxygen protecting group. In certain embodiments, each oxygen atom substituents is independently substituted (e.g., substituted with one or more halogen) or unsubstituted C1-6alkyl, −C(=O)Raa, −CO2Raa, −C(=O)N(Rbb)2, or an oxygen protecting group, wherein Raais hydrogen, substituted (e.g., substituted with one or more halogen) or unsubstituted C1-10 alkyl, or an oxygen protecting group when attached to an oxygen atom; and each Rbbis independently hydrogen, substituted (e.g., substituted with one or more halogen) or #13447332v2 unsubstituted C1-10 alkyl, or a nitrogen protecting group. In certain embodiments, each oxygen atom substituent is independently substituted (e.g., substituted with one or more halogen) or unsubstituted C1-6alkyl or an oxygen protecting group. In certain embodiments, the substituent present on an oxygen atom is an oxygen protecting group (also referred to herein as an “hydroxyl protecting group”). Oxygen protecting include −Raa, −N(Rbb)2, −C(=O)SRaa, −C(=O)Raa, −CO2Raa, −C(=O)N(Rbb)2, in the art and include those described in detail in Protecting Groups in Organic Synthesis, T. W. Greene and P. G. M. Wuts, 3rdedition, John Wiley & Sons, 1999, incorporated herein by reference. In certain embodiments, each oxygen protecting group, together with the oxygen atom to which the oxygen protecting group is attached, is selected from the group consisting of methyl, methoxymethyl (MOM), methylthiomethyl (MTM), t-butylthiomethyl, (phenyldimethylsilyl)methoxymethyl (SMOM), benzyloxymethyl (BOM), p- methoxybenzyloxymethyl (PMBM), (4-methoxyphenoxy)methyl (p-AOM), guaiacolmethyl (GUM), t-butoxymethyl, 4-pentenyloxymethyl (POM), siloxymethyl, 2-methoxyethoxymethyl (MEM), 2,2,2-trichloroethoxymethyl, bis(2-chloroethoxy)methyl, 2- (trimethylsilyl)ethoxymethyl (SEMOR), tetrahydropyranyl (THP), 3-bromotetrahydropyranyl, tetrahydrothiopyranyl, 1-methoxycyclohexyl, 4-methoxytetrahydropyranyl (MTHP), 4- methoxytetrahydrothiopyranyl, 4-methoxytetrahydrothiopyranyl S,S-dioxide, 1-[(2-chloro-4- methyl)phenyl]-4-methoxypiperidin-4-yl (CTMP), 1,4-dioxan-2-yl, tetrahydrofuranyl, tetrahydrothiofuranyl, 2,3,3a,4,5,6,7,7a-octahydro-7,8,8-trimethyl-4,7-methanobenzofuran-2-yl, 1-ethoxyethyl, 1-(2-chloroethoxy)ethyl, 1-methyl-1-methoxyethyl, 1-methyl-1-benzyloxyethyl, 1-methyl-1-benzyloxy-2-fluoroethyl, 2,2,2-trichloroethyl, 2-trimethylsilylethyl, 2- (phenylselenyl)ethyl, t-butyl, allyl, p-chlorophenyl, p-methoxyphenyl, 2,4-dinitrophenyl, benzyl (Bn), p-methoxybenzyl (PMB), 3,4-dimethoxybenzyl, o-nitrobenzyl, p-nitrobenzyl, p- halobenzyl, 2,6-dichlorobenzyl, p-cyanobenzyl, p-phenylbenzyl, 2-picolyl, 4-picolyl, 3-methyl- 2-picolyl N-oxido, diphenylmethyl, p,p’-dinitrobenzhydryl, 5-dibenzosuberyl, triphenylmethyl, α-naphthyldiphenylmethyl, p-methoxyphenyldiphenylmethyl, di(p- methoxyphenyl)phenylmethyl, tri(p-methoxyphenyl)methyl, 4-(4’- bromophenacyloxyphenyl)diphenylmethyl, 4,4′,4″-tris(4,5-dichlorophthalimidophenyl)methyl, 4,4′,4″-tris(levulinoyloxyphenyl)methyl, 4,4′,4″-tris(benzoyloxyphenyl)methyl, 4,4’-Dimethoxy- 3"‘-[N-(imidazolylmethyl) ]trityl Ether (IDTr-OR), 4,4’-Dimethoxy-3"‘-[N- #13447332v2 (imidazolylethyl)carbamoyl]trityl Ether (IETr-OR), 1,1-bis(4-methoxyphenyl)-1′-pyrenylmethyl, 9-anthryl, 9-(9-phenyl)xanthenyl, 9-(9-phenyl-10-oxo)anthryl, 1,3-benzodithiolan-2-yl, benzisothiazolyl S,S-dioxido, trimethylsilyl (TMS), triethylsilyl (TES), triisopropylsilyl (TIPS), dimethylisopropylsilyl (IPDMS), diethylisopropylsilyl (DEIPS), dimethylthexylsilyl, t- butyldimethylsilyl (TBDMS), t-butyldiphenylsilyl (TBDPS), tribenzylsilyl, tri-p-xylylsilyl, triphenylsilyl, diphenylmethylsilyl (DPMS), t-butylmethoxyphenylsilyl (TBMPS), formate, benzoylformate, acetate, chloroacetate, dichloroacetate, trichloroacetate, trifluoroacetate, methoxyacetate, triphenylmethoxyacetate, phenoxyacetate, p-chlorophenoxyacetate, 3- phenylpropionate, 4-oxopentanoate (levulinate), 4,4-(ethylenedithio)pentanoate (levulinoyldithioacetal), pivaloate, adamantoate, crotonate, 4-methoxycrotonate, benzoate, p- phenylbenzoate, 2,4,6-trimethylbenzoate (mesitoate), methyl carbonate, 9-fluorenylmethyl carbonate (Fmoc), ethyl carbonate, 2,2,2-trichloroethyl carbonate (Troc), 2-(trimethylsilyl)ethyl carbonate (TMSEC), 2-(phenylsulfonyl) ethyl carbonate (Psec), 2-(triphenylphosphonio) ethyl carbonate (Peoc), isobutyl carbonate, vinyl carbonate, allyl carbonate, t-butyl carbonate (BOC or Boc), p-nitrophenyl carbonate, benzyl carbonate, p-methoxybenzyl carbonate, 3,4- dimethoxybenzyl carbonate, o-nitrobenzyl carbonate, p-nitrobenzyl carbonate, S-benzyl thiocarbonate, 4-ethoxy-1-napththyl carbonate, methyl dithiocarbonate, 2-iodobenzoate, 4- azidobutyrate, 4-nitro-4-methylpentanoate, o-(dibromomethyl)benzoate, 2- formylbenzenesulfonate, 2-(methylthiomethoxy)ethyl carbonate (MTMEC-OR), 4- (methylthiomethoxy)butyrate, 2-(methylthiomethoxymethyl)benzoate, 2,6-dichloro-4- methylphenoxyacetate, 2,6-dichloro-4-(1,1,3,3-tetramethylbutyl)phenoxyacetate, 2,4-bis(1,1- dimethylpropyl)phenoxyacetate, chlorodiphenylacetate, isobutyrate, monosuccinoate, (E)-2- methyl-2-butenoate, o-(methoxyacyl)benzoate, α-naphthoate, nitrate, alkyl N,N,N’,N’- tetramethylphosphorodiamidate, alkyl N-phenylcarbamate, borate, dimethylphosphinothioyl, alkyl 2,4-dinitrophenylsulfenate, sulfate, methanesulfonate (mesylate), benzylsulfonate, and tosylate (Ts). In certain embodiments, at least one oxygen protecting group is silyl, TBDPS, TBDMS, TIPS, TES, TMS, MOM, THP, t-Bu, Bn, allyl, acetyl, pivaloyl, or benzoyl. In certain embodiments, each sulfur atom substituent is independently substituted (e.g., substituted with one or more halogen) or unsubstituted C1-10 alkyl, −C(=O)Raa, −CO2Raa, −C(=O)N(Rbb)2, or a sulfur protecting group. In certain embodiments, each sulfur atom substituent is independently substituted (e.g., substituted with one or more halogen) or unsubstituted C1-10alkyl, −C(=O)Raa, −CO2Raa, −C(=O)N(Rbb)2, or a sulfur protecting group, wherein Raais hydrogen, substituted (e.g., substituted with one or more halogen) or unsubstituted C1-10 alkyl, or an oxygen protecting group when attached to an oxygen atom; and #13447332v2 each Rbbis independently hydrogen, substituted (e.g., substituted with one or more halogen) or unsubstituted C1-10alkyl, or a nitrogen protecting group. In certain embodiments, each sulfur atom substituent is independently substituted (e.g., substituted with one or more halogen) or unsubstituted C1-6 alkyl or a sulfur protecting group. In certain embodiments, the substituent present on a sulfur atom is a sulfur protecting group (also referred to as a “thiol protecting group”). In some embodiments, each sulfur protecting group is selected from the group consisting of −Raa, −N(Rbb)2, −C(=O)SRaa, −C(=O)Raa, −CO2Raa, −C(=O)N(Rbb)2, −C(=NRbb)Raa, −C(=NRbb)ORaa, −C(=NRbb)N(Rbb)2, 2, −P(=O)(ORcc)2, and −P(=O)(N(Rbb) 2)2, wherein Raa, Rbb, and Rccare as defined herein. Sulfur protecting groups are well known in the art and include those described in detail in Protecting Groups in Organic Synthesis, T. W. Greene and P. G. M. Wuts, 3rdedition, John Wiley & Sons, 1999, incorporated herein by reference. In certain embodiments, the molecular weight of a substituent is lower than 250, lower than 200, lower than 150, lower than 100, or lower than 50 g / mol. In certain embodiments, a substituent consists of carbon, hydrogen, fluorine, chlorine, bromine, iodine, oxygen, sulfur, nitrogen, and / or silicon atoms. In certain embodiments, a substituent consists of carbon, hydrogen, fluorine, chlorine, bromine, iodine, oxygen, sulfur, and / or nitrogen atoms. In certain embodiments, a substituent consists of carbon, hydrogen, fluorine, chlorine, bromine, and / or iodine atoms. In certain embodiments, a substituent consists of carbon, hydrogen, fluorine, and / or chlorine atoms. In certain embodiments, a substituent comprises 0, 1, 2, or 3 hydrogen bond donors. In certain embodiments, a substituent comprises 0, 1, 2, or 3 hydrogen bond acceptors. A “counterion” or “anionic counterion” is a negatively charged group associated with a positively charged group in order to maintain electronic neutrality. An anionic counterion may be monovalent (e.g., including one formal negative charge). An anionic counterion may also be multivalent (e.g., including more than one formal negative charge), such as divalent or trivalent. Exemplary counterions include halide ions (e.g., F–, Cl–, Br–, I–), NO3–, ClO4–, OH–, H2PO4–, HCO3−,HSO4–, sulfonate ions (e.g., methansulfonate, trifluoromethanesulfonate, p– toluenesulfonate, benzenesulfonate, 10–camphor sulfonate, naphthalene–2–sulfonate, naphthalene–1–sulfonic acid–5–sulfonate, ethan–1–sulfonic acid–2–sulfonate, and the like), carboxylate ions (e.g., acetate, propanoate, benzoate, glycerate, lactate, tartrate, glycolate, gluconate, and the like), BF4−, PF4–, PF6–, AsF6–, SbF6–, B[3,5-(CF3)2C6H3]4]–, B(C6F5)4−, BPh4–, Al(OC(CF3)3)4–, and carborane anions (e.g., CB11H12–or (HCB11Me5Br6)–). Exemplary counterions which may be multivalent include CO32−, HPO42−, PO 3− 4 , B4O72−, SO42−, S2O32−, #13447332v2 carboxylate anions (e.g., tartrate, citrate, fumarate, maleate, malate, malonate, gluconate, succinate, glutarate, adipate, pimelate, suberate, azelate, sebacate, salicylate, phthalates, aspartate, glutamate, and the like), and carboranes. Use of the phrase “at least one instance” refers to 1, 2, 3, 4, or more instances, but also encompasses a range, e.g., for example, from 1 to 4, from 1 to 3, from 1 to 2, from 2 to 4, from 2 to 3, or from 3 to 4 instances, inclusive. A “non-hydrogen group” refers to any group that is defined for a particular variable that is not hydrogen. The term “pharmaceutically acceptable salt” refers to those salts which are, within the scope of sound medical judgment, suitable for use in contact with the tissues of humans and lower animals without undue toxicity, irritation, allergic response, and the like, and are commensurate with a reasonable benefit / risk ratio. Pharmaceutically acceptable salts are well known in the art. For example, Berge et al. describe pharmaceutically acceptable salts in detail in J. Pharmaceutical Sciences, 1977, 66, 1-19, incorporated herein by reference. Pharmaceutically acceptable salts of the compounds of this disclosure include those derived from suitable inorganic and organic acids and bases. Examples of pharmaceutically acceptable, nontoxic acid addition salts are salts of an amino group formed with inorganic acids, such as hydrochloric acid, hydrobromic acid, phosphoric acid, sulfuric acid, and perchloric acid or with organic acids, such as acetic acid, oxalic acid, maleic acid, tartaric acid, citric acid, succinic acid, or malonic acid or by using other methods known in the art such as ion exchange. Other pharmaceutically acceptable salts include adipate, alginate, ascorbate, aspartate, benzenesulfonate, benzoate, bisulfate, borate, butyrate, camphorate, camphorsulfonate, citrate, cyclopentanepropionate, digluconate, dodecylsulfate, ethanesulfonate, formate, fumarate, glucoheptonate, glycerophosphate, gluconate, hemisulfate, heptanoate, hexanoate, hydroiodide, 2-hydroxy-ethanesulfonate, lactobionate, lactate, laurate, lauryl sulfate, malate, maleate, malonate, methanesulfonate, 2-naphthalenesulfonate, nicotinate, nitrate, oleate, oxalate, palmitate, pamoate, pectinate, persulfate, 3-phenylpropionate, phosphate, picrate, pivalate, propionate, stearate, succinate, sulfate, tartrate, thiocyanate, p-toluenesulfonate, undecanoate, valerate salts, and the like. Salts derived from appropriate bases include alkali metal, alkaline earth metal, ammonium, and N+(C1-4 alkyl)4 salts. Representative alkali or alkaline earth metal salts include sodium, lithium, potassium, calcium, magnesium, and the like. Further pharmaceutically acceptable salts include, when appropriate, nontoxic ammonium, quaternary ammonium, and amine cations formed using counterions such as halide, hydroxide, carboxylate, sulfate, phosphate, nitrate, lower alkyl sulfonate, and aryl sulfonate. #13447332v2 The term “solvate” refers to forms of the compound, or a salt thereof, that are associated with a solvent, usually by a solvolysis reaction. This physical association may include hydrogen bonding. Conventional solvents include water, methanol, ethanol, acetic acid, DMSO, THF, diethyl ether, and the like. The compounds described herein may be prepared, e.g., in crystalline form, and may be solvated. Suitable solvates include pharmaceutically acceptable solvates and further include both stoichiometric solvates and non-stoichiometric solvates. In certain instances, the solvate will be capable of isolation, for example, when one or more solvent molecules are incorporated in the crystal lattice of a crystalline solid. “Solvate” encompasses both solution-phase and isolatable solvates. Representative solvates include hydrates, ethanolates, and methanolates. The term “hydrate” refers to a compound that is associated with water. Typically, the number of the water molecules contained in a hydrate of a compound is in a definite ratio to the number of the compound molecules in the hydrate. Therefore, a hydrate of a compound may be represented, for example, by the general formula R⋅x H2O, wherein R is the compound, and x is a number greater than 0. A given compound may form more than one type of hydrate, including, e.g., monohydrates (x is 1), lower hydrates (x is a number greater than 0 and smaller than 1, e.g., hemihydrates (R⋅0.5 H2O)), and polyhydrates (x is a number greater than 1, e.g., dihydrates (R⋅2 H2O) and hexahydrates (R⋅6 H2O)). The term “tautomers” or “tautomeric” refers to two or more interconvertible compounds resulting from at least one formal migration of a hydrogen atom and at least one change in valency (e.g., a single bond to a double bond, a triple bond to a single bond, or vice versa). The exact ratio of the tautomers depends on several factors, including temperature, solvent, and pH. Tautomerizations (i.e., the reaction providing a tautomeric pair) may catalyzed by acid or base. Exemplary tautomerizations include keto-to-enol, amide-to-imide, lactam-to-lactim, enamine-to- imine, and enamine-to-(a different enamine) tautomerizations. It is also to be understood that compounds that have the same molecular formula but differ in the nature or sequence of bonding of their atoms or the arrangement of their atoms in space are termed “isomers”. Isomers that differ in the arrangement of their atoms in space are termed “stereoisomers”. Stereoisomers that are not mirror images of one another are termed “diastereomers” and those that are non-superimposable mirror images of each other are termed “enantiomers”. When a compound has an asymmetric center, for example, it is bonded to four different groups, a pair of enantiomers is possible. An enantiomer can be characterized by the absolute configuration of its asymmetric center and is described by the R- and S-sequencing rules of Cahn and Prelog, or by the manner in which the molecule rotates the plane of polarized light and designated as #13447332v2 dextrorotatory or levorotatory (i.e., as (+) or (−)-isomers respectively). A chiral compound can exist as either individual enantiomer or as a mixture thereof. A mixture containing equal proportions of the enantiomers is called a “racemic mixture”. The term “crystalline” or “crystalline form” refers to a solid form substantially exhibiting three-dimensional order. In certain embodiments, a crystalline form of a solid is a solid form that is substantially not amorphous. In certain embodiments, the X-ray powder diffraction (XRPD) pattern of a crystalline form includes one or more sharply defined peaks. The term “co-crystal” refers to a crystalline structure comprising at least two different components (e.g., a compound disclosed herein and an acid), wherein each of the components is independently an atom, ion, or molecule. In certain embodiments, none of the components is a solvent. In certain embodiments, at least one of the components is a solvent. A co-crystal of a compound disclosed herein and an acid is different from a salt formed from a compound disclosed herein and the acid. In the salt, a compound disclosed herein is complexed with the acid in a way that proton transfer (e.g., a complete proton transfer) from the acid to a compound disclosed herein easily occurs at room temperature. In the co-crystal, however, a compound disclosed herein is complexed with the acid in a way that proton transfer from the acid to a compound disclosed herein does not easily occur at room temperature. In certain embodiments, in the co-crystal, there is no proton transfer from the acid to a compound disclosed herein. In certain embodiments, in the co-crystal, there is partial proton transfer from the acid to a compound disclosed herein. Co-crystals may be useful to improve the properties (e.g., solubility, stability, and ease of formulation) of a compound disclosed herein. The term “polymorph” refers to a crystalline form of a compound (or a salt, hydrate, or solvate thereof). All polymorphs have the same elemental composition. Different crystalline forms usually have different X-ray diffraction patterns, infrared spectra, melting points, density, hardness, crystal shape, optical and electrical properties, stability, and solubility. Recrystallization solvent, rate of crystallization, storage temperature, and other factors may cause one crystal form to dominate. Various polymorphs of a compound can be prepared by crystallization under different conditions. The term “small molecule” refers to molecules, whether naturally occurring or artificially created (e.g., via chemical synthesis) that have a relatively low molecular weight. Typically, a small molecule is an organic compound (e.g., it contains carbon). The small molecule may contain multiple carbon-carbon bonds, stereocenters, and other functional groups (e.g., amines, hydroxyl, carbonyls, and heterocyclic rings, etc.). In certain embodiments, the molecular weight of a small molecule is not more than about 1,000 g / mol, not more than about 900 g / mol, not more than about 800 g / mol, not more than about 700 g / mol, not more than about 600 g / mol, not #13447332v2 more than about 500 g / mol, not more than about 400 g / mol, not more than about 300 g / mol, not more than about 200 g / mol, or not more than about 100 g / mol. In certain embodiments, the molecular weight of a small molecule is at least about 100 g / mol, at least about 200 g / mol, at least about 300 g / mol, at least about 400 g / mol, at least about 500 g / mol, at least about 600 g / mol, at least about 700 g / mol, at least about 800 g / mol, or at least about 900 g / mol, or at least about 1,000 g / mol. Combinations of the above ranges (e.g., at least about 200 g / mol and not more than about 500 g / mol) are also possible. In certain embodiments, the small molecule is a therapeutically active agent such as a drug (e.g., a molecule approved by the U.S. Food and Drug Administration as provided in the Code of Federal Regulations (C.F.R.)). The small molecule may also be complexed with one or more metal atoms and / or metal ions. In this instance, the small molecule is also referred to as a “small organometallic molecule.” Preferred small molecules are biologically active in that they produce a biological effect in animals, preferably mammals, more preferably humans. Small molecules include, but are not limited to, radionuclides and imaging agents. In certain embodiments, the small molecule is a drug. Preferably, though not necessarily, the drug is one that has already been deemed safe and effective for use in humans or animals by the appropriate governmental agency or regulatory body. For example, drugs approved for human use are listed by the FDA under 21 C.F.R. §§ 330.5, 331 through 361, and 440 through 460, incorporated herein by reference; drugs for veterinary use are listed by the FDA under 21 C.F.R. §§ 500 through 589, incorporated herein by reference. All listed drugs are considered acceptable for use in accordance with the present disclosure. A “subject” to which administration is contemplated includes, but is not limited to, humans (i.e., a male or female of any age group, e.g., a pediatric subject (e.g., infant, child, adolescent) or adult subject (e.g., young adult, middle–aged adult, or senior adult)) and / or other non–human animals, for example, mammals (e.g., primates (e.g., cynomolgus monkeys, rhesus monkeys); commercially relevant mammals such as cattle, pigs, horses, sheep, goats, cats, and / or dogs) and birds (e.g., commercially relevant birds such as chickens, ducks, geese, and / or turkeys). In certain embodiments, the animal is a mammal. The animal may be a male or female and at any stage of development. A non–human animal may be a transgenic animal. The term “patient” refers to a human subject in need of treatment of a disease or disorder. The term “biological sample” refers to any sample including tissue samples (such as tissue sections and needle biopsies of a tissue); cell samples (e.g., cytological smears (such as Pap or blood smears) or samples of cells obtained by microdissection); samples of whole organisms (such as samples of yeasts or bacteria); or cell fractions, fragments, organelles (such as obtained by lysing cells and separating the components thereof by centrifugation or #13447332v2 otherwise). Other examples of biological samples include blood, serum, urine, semen, fecal matter, cerebrospinal fluid, interstitial fluid, mucus, tears, sweat, pus, biopsied tissue (e.g., obtained by a surgical biopsy or needle biopsy), nipple aspirates, milk, vaginal fluid, saliva, swabs (such as buccal swabs), or any material containing biomolecules that is derived from a first biological sample. Biological samples also include those biological samples that are transgenic, such as a transgenic oocyte, sperm cell, blastocyst, embryo, fetus, donor cell, or cell nucleus, or cells or cell lines derived from biological samples. The term “tissue” refers to any biological tissue of a subject (including a group of cells, a body part, or an organ) or a part thereof, including blood and / or lymph vessels, which is the object to which a compound, particle, and / or composition of the disclosure is delivered. A tissue may be an abnormal or unhealthy tissue, which may need to be treated. A tissue may also be a normal or healthy tissue that is under a higher than normal risk of becoming abnormal or unhealthy, which may need to be prevented. In certain embodiments, the tissue is the central nervous system. In certain embodiments, the tissue is the brain. The terms “administer,” “administering,” or “administration” refer to implanting, absorbing, ingesting, injecting, inhaling, or otherwise introducing a compound, or a pharmaceutical composition thereof. The terms “treatment,” “treat,” and “treating” refer to reversing, alleviating, delaying the onset of, or inhibiting the progress of a “pathological condition” (e.g., a disease, disorder, or condition, or one or more signs or symptoms thereof) described herein. In some embodiments, treatment may be administered after one or more signs or symptoms have developed or have been observed. In other embodiments, treatment may be administered in the absence of signs or symptoms of the disease or condition. For example, treatment may be administered to a susceptible individual prior to the onset of symptoms (e.g., in light of a history of symptoms and / or in light of genetic or other susceptibility factors). Treatment may also be continued after symptoms have resolved, for example, to delay or prevent recurrence. The terms “prevent,” “preventing,” or “prevention” refers to a prophylactic treatment of a subject who is not and was not with a disease or disorder but is at risk of developing the disease or disorder or who was with a disease or disorder, is not with the disease or disorder, but is at risk of regression of the disease or disorder. In certain embodiments, the subject is at a higher risk of developing the disease or disorder or at a higher risk of regression of the disease or disorder than an average healthy member of a population of subjects. The terms “condition,” “disease,” and “disorder” are used interchangeably. An “effective amount” of a compound described herein refers to an amount sufficient to elicit the desired biological response, i.e., treating the condition. As will be appreciated by those #13447332v2 of ordinary skill in this art, the effective amount of a compound described herein may vary depending on such factors as the desired biological endpoint, the pharmacokinetics of the compound, the condition being treated, the mode of administration, and the age and health of the subject. An effective amount encompasses therapeutic and prophylactic treatment. For example, in treating cancer, an effective amount of a compound may reduce the tumor burden or stop the growth or spread of a tumor. A “therapeutically effective amount” of a compound described herein is an amount sufficient to provide a therapeutic benefit in the treatment of a condition or to delay or minimize one or more symptoms associated with the condition. A therapeutically effective amount of a compound means an amount of therapeutic agent, alone or in combination with other therapies, which provides a therapeutic benefit in the treatment of the condition. The term “therapeutically effective amount” can encompass an amount that improves overall therapy, reduces, or avoids symptoms or causes of the condition, or enhances the therapeutic efficacy of another therapeutic agent. In certain embodiments, a therapeutically effective amount is an amount sufficient, e.g. for inhibiting a biological target (e.g., at least 5%, at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 95%, or at least 99% inhibition of the target). In certain embodiments, a therapeutically effective amount is an amount sufficient for treating a disease or condition. A “prophylactically effective amount” of a compound described herein is an amount sufficient to prevent a condition, or one or more signs or symptoms associated with the condition, or prevent its recurrence. A prophylactically effective amount of a compound means an amount of a therapeutic agent, alone or in combination with other agents, which provides a prophylactic benefit in the prevention of the condition. The term “prophylactically effective amount” can encompass an amount that improves overall prophylaxis or enhances the prophylactic efficacy of another prophylactic agent. The terms “therapeutic compound,” “therapeutic agent,” or “therapeutic moiety” refer to any substance having therapeutic properties that produce a desired, usually beneficial, effect. For example, therapeutic compounds, agents, and moieties may treat and / or ameliorate a disease or disorder. Therapeutic compounds, agents, and moieties, as disclosed herein, may be biologics or small molecule therapeutics, or combinations thereof. The term “sustained release” (also referred to as extended release or controlled release) refers to a continuous or continual release of a therapeutic agent introduced into the body of a subject over a period of time and at a therapeutic level sufficient to achieve a desired therapeutic effect throughout the period of time. The rate at which the therapeutic agent is released is slower than the rate of release of the therapeutic agent when it is administered alone or in a non- #13447332v2 sustained release formulation. Sustained release formulations may, by way of example, be created as films, slabs, pellets, microparticles, microspheres, microcapsules, spheroids, shaped derivatives and paste. The formulations may be in a form that is suitable for suspension in isotonic saline, physiological buffer or other solution acceptable for injection into a patient. Further, the formulations may be used in conjunction with any implantable, insertable or injectable system that a person of ordinary skill would appreciate as useful in connection with embodiments herein including but not limited to parenteral formulations, microspheres, microcapsules, gels, pastes, implantable rods, pellets, plates or fibers, etc. The term “particle” refers to a small object, fragment, or piece of a substance that may be a single element, inorganic material, organic material, or mixture thereof. Examples of particles include polymeric particles, single-emulsion particles, double-emulsion particles, coacervates, liposomes, microparticles, nanoparticles, macroscopic particles, pellets, crystals, aggregates, composites, pulverized, milled or otherwise disrupted matrices, and cross-linked protein or polysaccharide particles, each of which have an average characteristic dimension of about less than about 1 mm and at least 1 nm, where the characteristic dimension, or “critical dimension,” of the particle is the smallest cross-sectional dimension of the particle. A particle may be composed of a single substance or multiple substances. In certain embodiments, the particle is not a viral particle. In other embodiments, the particle is not a liposome. In certain embodiments, the particle is not a micelle. In certain embodiments, the particle is substantially solid throughout. In certain embodiments, the particle is a nanoparticle. In certain embodiments, the particle is a microparticle. The term “nanoparticle” refers to a particle having an average (e.g., mean) dimension (e.g., diameter) of between about 1 nanometer (nm) and about 1 micrometer (µm) (e.g., between about 1 nm and about 300 nm, between about 1 nm and about 100 nm, between about 1 nm and about 30 nm, between about 1 nm and about 10 nm, or between about 1 nm and about 3 nm), inclusive. The term “microparticle” refers to a particle having an average (e.g., mean) dimension (e.g., diameter) of between about 1 micrometer (µm) and about 1 millimeter (mm) (e.g., between about 1 µm and about 100 µm, between about 1 µm and about 30 µm, between about 1 µm and about 10 µm, or between about 1 µm and about 3 µm), inclusive. The “hydrodynamic diameter” of a particle refers to the diameter of a solid sphere that would exhibit the same hydrodynamic friction as the particle (e.g., the diameter of a solid sphere that diffuses at the same rate as the particle). Hydrodynamic diameter can be measured through various techniques including dynamic light scattering (DLS) and nanoparticle tracking analysis (NTA). #13447332v2 The term “protein-stabilized nanoparticle” refers to a nanoparticle that retains one or more properties (e.g., aggregation, composition, crystallinity, shape, size, surface chemistry) when associated (e.g., non-covalently associated or covalently associated) with a protein, compared to a nanoparticle that is not associated with a protein. In some embodiments, the one or more properties are retained for a longer duration of time. BRIEF DESCRIPTION OF DRAWINGS The accompanying drawings are not intended to be drawn to scale. In the drawings, each identical or nearly identical component that is illustrated in various figures is represented by a like numeral. For purposes of clarity, not every component may be labeled in every drawing. In the drawings: FIG.1 shows a synthetic scheme of BNP@BSA-X, a glutaraldehyde-crosslinked bovine serum albumin hydrogel (BSA-X) containing bupivacaine free base nanoparticles (BNPs). FIGs.2A-2E show characterization of BNP@BSA-X. FIG.2A shows size distribution by volume percent of BSA and BNP@BSA measured by dynamic light scattering (DLS). FIG. 2B shows Transmission electron micrograph (TEM) of BNP@BSA. Scale bar: 100nm. FIG.2C shows comparison of the storage moduli (G') at an angular frequency of 102rad / s for BNP@BSA-X with varying concentrations of BSA and GA. The selection of 102rad / s is based on its falling within the range associated with muscle tremor and vibration (62.83-251.3 rad / s). FIG.2D shows mechanical properties of BNP@BSA-X (50:5; 50mg / ml of BSA and 5mg / ml of GA) determined by rheometry in response to the repeated shear strain. Strain was applied at 0.1% for 60 seconds (white regions), followed by 500% for 60 seconds (grey regions). This was repeated three times. FIG.2E shows cumulative bupivacaine release (as the percent of total amount loaded) from formulations. Data are means ± SD (n = 4). FIG.3 shows cumulative drug release (as a percentage of the total loaded amount) from free drugs (diphenhydramine•HCl and paclitaxel) and their corresponding nanoparticles in BSA- X. Data are means ± SD (n = 4). p-values compare groups at 24 h. FIG.4 shows sciatic nerve blockade. Sensory block duration from bupivacaine•HCl (5 mg / ml), and various concentrations of bupivacaine nanoparticles in uncrosslinked and crosslinked BSA (BNP@BSA and BNP@BSA-X, respectively) is shown. Also shown are the durations of block from, bupivacaine•HCl@BSA-X (20 mg / ml), and EXPAREL® (13.3mg / ml). Data are means ± SD (n = 4-9). p-values compare groups at 20 mg / ml of bupivacaine. FIGs.5A-5D show tissue retention of fluorescently labeled formulations injected at the sciatic nerve, detected by IVIS. FIG.5A shows representative time courses of retention of ICG dye containing formulations FIG.5B shows quantification of the fluorescence intensity over #13447332v2 time, derived from data such as those in FIG.5A. Data are means ± SD (n = 4). p-values compare groups at 28 days. FIG.5C shows representative time courses of retention of Cy5.5 containing formulations. FIG.5D shows quantification of the fluorescence intensity over time, derived from data such as those in FIG.5C. Bupivacaine concentration was 20 mg / ml. Data are means ± SD (n = 4). p-values compare groups at 7 days. FIGs.6A-6B show comparison of tissue retention and the duration of sensory nerve block for different formulations. FIG.5A shows duration of block as a function of the half-life of tissue retention of ICG, calculated from data in FIG.5B. FIG.6B shows Tissue retention of Cy5.5 on day 2, calculated from the data in FIG.5D. FIGs.7A-7E show tissue reaction. Representative hematoxylin-eosin stained sections of muscles and nerve 4 days after injection of (FIGs.7A-7B) BNP@BSA-X with 20 mg / ml bupivacaine or (FIGs.7C-7D) EXPAREL®. Scale bar: 200 µm (magnification 100x, FIGs.7A and 7C), 40 µm (magnification 400x, FIGs.7B and 7D). M: muscle, Mtox: myotoxicity, N: nerve, Infl: inflammation, BSA-X: crosslinked BSA. FIG.7E shows scores for tissue reaction on day 4. Data are medians with interquartile ranges (n = 4-6). p values are calculated from Mann- Whitney U test. FIG.8 shows a photograph of BNP, BNP@BSA and BNP@BSA-X. Ratios represent concentrations of BSA (mg / ml): GA (mg / ml). Bupivacaine concentration was set at 20 mg / ml. The cross-linked samples (BSA-X) formed hydrogels, as evidence by the fact that they did not flow down inverted tubes FIG.9 shows gelation time (the time after the addition of GA for storage moduli to plateau) of BNP@BSA-X with different concentrations of BSA and GA, determined by rheometry. The gelation time was recorded over a 5-hour period at a frequency of 6.28 rad / s and a strain of 0.1%. Data are means ± SD (n = 3). FIG.10 shows mechanical properties of BNP@BSA-X with different concentrations of BSA and GA determined by rheometry in response to the angular frequency sweeps. The range of angular frequency was 0.63 to 628 rad s−1with the strain of 0.1%. FIG.11 shows mechanical properties of BNP@BSA-X (50:10; 50mg / ml of BSA and 10mg / ml of GA) determined by rheometry in response to the repeated shear strain. Strain was applied at 0.1% for 60 seconds (white regions), followed by 500% (grey regions), repeated for three cycles. FIG.12 shows surface morphology of BNP@BSA-X using scanning electron microscopy (SEM). Scale bar: 8 µm. FIGs.13A-13C show DNP@BSA-X: A hydrogel derived from glutaraldehyde- crosslinked bovine serum albumin (BSA-X) encapsulating drug nanoparticles (DNPs). FIG.13A #13447332v2 shows synthetic scheme for DNP@BSA-X incorporating either amphiphilic (diphenhydramine) or hydrophobic (paclitaxel) drugs. FIG.13B shows transmission electron microscopy (TEM) images of DHNP@BSA (left panel; Scale bar: 100nm) and PNP@BSA (right panel; Scale bar: 500nm). FIG.13C shows mechanical properties of DHNP@BSA-X and PNP@BSA-X determined by rheometry. FIGs.14A-14B show comparison of the durations of sensory and motor block of various formulation at various bupivacaine concentrations. FIG.14A shows BNP@BSA and BNP@BSA-X. FIG.14B shows Bupivacaine•HCl, Exparel®, and bupivacaine•HCl @BSA-X 20 mg / ml. Note the difference in the magnitude of the axes between the panels. The diagonal dashed line indicates equal durations of sensory and motor neve block. Data are means ± SD (n = 4-9). FIGs.15A-15B show representative images showing the ability of BSA to prevent the aggregation of bupivacaine free base (20 mg / ml). (A) Bupivacaine free base added to PBS. When the vial was inverted, bupivacaine free base adhered to the walls (arrow). (B) Bupivacaine free base added to BSA solution (50 mg / mL) in PBS. No bupivacaine free base adhered to the vial wall. FIG.16 shows fluorescent emission spectra of BSA solution with different concentrations of BNP using fluorescence spectroscopy. Excitation: 280 nm, Emission: 310–450 nm. FIG.17 shows UV-visible absorbance spectra (190-350 nm) of BSA solution with different concentrations of BNP. The spectrum for 0.08 mg / ml BNP in PBS is also shown. FIGS.18A-18B show representative hematoxylin-eosin stained sections of muscles 28 days after injection of BNP@BSA-X with 20 mg / ml bupivacaine. (FIG.18A) Scale bar: 200 µm (magnification 100X) (FIG.18B) Scale bar: 40 µm (magnification 400X). FIG.19 shows thermal latency in uninjected animals (“uninjected”) and in the uninjected (contralateral) hind paw when each formulation was injected into the other leg. The graph shows the thermal latency at the representative time point of 1 hr post-injection. Thermal latencies of uninjected legs were measured throughout the study, and none of the formulations caused deficits in the uninjected hind paw during the entire study period. Data are means ± SD (n = 4- 9). DETAILED DESCRIPTION Provided herein is a hybrid nanoparticle-hydrogel approach to extending the therapeutic effect of drugs including, but not limited to, local anesthetics (e.g., bupivacaine). In an embodiment, bupivacaine was self-assembled in the hydrophobic free base form into #13447332v2 nanoparticles to maximize loading and slow release of the drug. The bupivacaine nanoparticles were formed in the presence of bovine serum albumin (BSA) to enhance nanoparticle stability and prevent aggregation. Since BSA also binds hydrophobic drugs such as bupivacaine, it may contribute to slow release of the drug. Moreover, BSA is cross-linked to create a macroscopic hydrogel, further slowing the release of bupivacaine, and maintaining the nanoparticles at the site of administration. Accordingly, increased loading and extended release of drug was achieved by nanoparticles of carrier-free hydrophobic bupivacaine in a cross-linked albumin matrix, leading to an unexpectedly long duration of extended nerve block in vivo. Furthermore, the reduction in release rate mitigates local tissue injury observed in existing formulations. The present disclosure provides a composition comprising a hydrogel and a protein- stabilized particle, wherein: the hydrogel comprises a crosslinked protein matrix; the protein-stabilized particle comprises a therapeutic agent or a diagnostic agent; and the protein-stabilized particle is embedded in the crosslinked protein matrix. In some embodiments, the protein-stabilized particle is a protein-stabilized nanoparticle. In some embodiments, the protein-stabilized particle is a protein-stabilized microparticle. The present disclosure also provides a composition comprising a hydrogel and a particle, wherein: the hydrogel comprises a crosslinked protein matrix; the particle comprises an anesthetic; and the particle is embedded in the crosslinked protein matrix. In some embodiments, the particle is a nanoparticle. In some embodiments, the particle is a microparticle. The present disclosure also provides a composition comprising a hydrogel and a protein- stabilized nanoparticle, wherein: the hydrogel comprises a crosslinked protein matrix; the protein-stabilized nanoparticle comprises a therapeutic agent or a diagnostic agent; and the protein-stabilized nanoparticle is embedded in the crosslinked protein matrix. The present disclosure also provides a composition comprising a hydrogel and a nanoparticle, wherein: the hydrogel comprises a crosslinked protein matrix; the nanoparticle comprises an anesthetic; and the nanoparticle is embedded in the crosslinked protein matrix. #13447332v2 As described herein, the composition comprises a hydrogel and a protein-stabilized nanoparticle, or the composition comprises a hydrogel and a nanoparticle. In some embodiments, the composition comprises additional components. Hydrogel As described herein, the hydrogel comprises a crosslinked protein matrix. In some embodiments, the hydrogel comprises saline. In some embodiments, the hydrogel comprises a buffer. In some embodiments, the hydrogel comprises pH 7.4 phosphate-buffered saline (PBS). In some embodiments, the hydrogel comprises a buffer with a pH of about 1, about 2, about 3, about 4, about 5, about 6, about 7, about 8, about 9, about 10, about 11, about 12, about 13, or about 14. In some embodiments, the hydrogel comprises a buffer with a pH of about 4, about 4.5, about 5, about 5.5, about 6, about 6.5, about 7, about 7.5, about 8, about 8.5, about 9, about 9.5, or about 10. In some embodiments, the hydrogel comprises a buffer with a pH of about 7.4. In some embodiments, the hydrogel comprises a buffer with a pH of between about 1 and about 14, between about 2 and about 13, between about 3 and about 12, between about 4 and about 11, between about 5 and about 10, between about 6 and about 9, or between about 7 and about 8. In some embodiments, the hydrogel comprises a buffer with a pH of between about 5 and about 9, between about 5 and about 8.5, between about 5 and about 8, between about 5 and about 7.5, between about 5 and about 7, between about 5 and about 6.5, between about 5 and about 6, between about 5.5 and about 9, between about 5.5 and about 8.5, between about 5.5 and about 8, between about 5.5 and about 7.5, between about 5.5 and about 7, between about 5.5 and about 6.5, between about 5.5 and about 6, between about 6 and about 9, between about 6 and about 8.5, between about 6 and about 8, between about 6 and about 7.5, between about 6 and about 7, between about 6 and about 6.5, between about 6.5 and about 9, between about 6.5 and about 8.5, between about 6.5 and about 8, between about 6.5 and about 7.5, between about 6.5 and about 7, between about 7 and about 9, between about 7 and about 8.5, between about 7 and about 8, between about 7 and about 7.5, between about 7.5 and about 9, between about 7.5 and about 8.5, between about 7.5 and about 8, between about 8 and about 9, between about 8 and about 8.5, or between about 8.5 and about 9. In some embodiments, the hydrogel comprises a buffer with a pH of between about 4 and about 11, between about 5 and about 10, between about 6 and about 9, or between about 7 and about 8. Crosslinked Protein Matrix In some embodiments, the crosslinked protein matrix comprises a crosslinked protein. In some embodiments, the crosslinked protein is crosslinked bovine serum albumin or crosslinked alpha-1-acid glycoprotein. In some embodiments, the crosslinked protein is crosslinked bovine #13447332v2 serum albumin. In some embodiments, the crosslinked protein is crosslinked alpha-1-acid glycoprotein. In some embodiments, the crosslinked protein matrix is non-covalently crosslinked. In some embodiments, the crosslinked protein matrix is covalently crosslinked. In some embodiments, the crosslinked protein is covalently crosslinked bovine serum albumin or covalently crosslinked alpha-1-acid glycoprotein. In some embodiments, the crosslinked protein is covalently crosslinked bovine serum albumin. In some embodiments, the crosslinked protein is covalently crosslinked alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent (e.g., bupivacaine) is capable of binding to the crosslinked protein. In some embodiments, the therapeutic agent (e.g., bupivacaine) is capable of binding to crosslinked bovine serum albumin or crosslinked alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent (e.g., bupivacaine) is capable of binding to crosslinked bovine serum albumin. In some embodiments, the therapeutic agent (e.g., bupivacaine) is capable of binding to crosslinked alpha-1-acid glycoprotein. Formula (I) In some embodiments, the crosslinked protein matrix comprises a moiety of Formula (I): wherein: each instance of Z is independently a protein in the crosslinked protein matrix; and L is optionally substituted alkylene or optionally substituted heteroalkylene. In some embodiments, at least one instance of Z is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, at least one instance of Z is bovine serum albumin. In some embodiments, at least one instance of Z is alpha-1-acid glycoprotein. In some embodiments, each instance of Z is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, each instance of Z is bovine serum albumin. In some embodiments, each instance of Z is alpha- 1-acid glycoprotein. In some embodiments, each instance of Z is a different instance of the protein in the crosslinked protein matrix. In some embodiments, L is optionally substituted alkylene. In some embodiments, L is optionally substituted C1-12alkylene. In some embodiments, L is optionally substituted C1-6alkylene. In some embodiments, L is optionally substituted C1-3 alkylene. In some embodiments, L is optionally substituted C12 alkylene, optionally substituted C11 alkylene, optionally substituted C10alkylene, optionally substituted C9alkylene, optionally #13447332v2 substituted C8 alkylene, optionally substituted C7 alkylene, optionally substituted C6 alkylene, optionally substituted C5alkylene, optionally substituted C4alkylene, optionally substituted C3alkylene, optionally substituted C2alkylene, or optionally substituted C1alkylene. In some embodiments, L is optionally substituted C12 alkylene. In some embodiments, L is optionally substituted C11 alkylene. In some embodiments, L is optionally substituted C10 alkylene. In some embodiments, L is optionally substituted C9alkylene. In some embodiments, L is optionally substituted C8 alkylene. In some embodiments, L is optionally substituted C7 alkylene. In some embodiments, L is optionally substituted C6 alkylene. In some embodiments, L is optionally substituted C5alkylene. In some embodiments, L is optionally substituted C4alkylene. In some embodiments, L is optionally substituted C3 alkylene. In some embodiments, L is optionally substituted C2 alkylene. In some embodiments, L is optionally substituted C1 alkylene. In some embodiments, L is substituted alkylene. In some embodiments, L is substituted C1-12alkylene. In some embodiments, L is substituted C1-6alkylene. In some embodiments, L is substituted C1-3 alkylene. In some embodiments, L is alkylene (e.g., C1-12 alkylene, C1-6 alkylene, C1-3 alkylene) substituted with halogen, optionally substituted alkyl, optionally substituted alkenyl, optionally substituted alkynyl, optionally substituted heteroalkyl, optionally substituted heteroalkenyl, optionally substituted heteroalkynyl, optionally substituted carbocyclyl, optionally substituted heterocyclyl, optionally substituted aryl, optionally substituted heteroaryl, –CN, –ORA, –SCN, –SRA, –SSRA, –N3, –NO, –N(RA)2, –NO2, –C(=O)RA, –C(=O)ORA, –C(=O)SRA, –C(=O)N(RA)2, –C(=NRA)RA, –C(=NRA)ORA, –C(=NRA)SRA, –C(=NRA)N(RA)2, –S(=O)RA, –S(=O)ORA, –S(=O)SRA, –S(=O)N(RA)2, –S(=O)2RA, –S(=O)2ORA, –S(=O)2SRA, –S(=O)2N(RA)2, –OC(=O)RA, –OC(=O)ORA, –OC(=O)SRA, –OC(=O)N(RA)2, –OC(=NRA)RA, –OC(=NRA)ORA, –OC(=NRA)SRA, –OC(=NRA)N(RA)2, –OS(=O)RA, –OS(=O)ORA, –OS(=O)SRA, –OS(=O)N(RA)2, –OS(=O)2RA, –OS(=O)2ORA, –OS(=O)2SRA, –OS(=O)2N(RA)2, –ON(RA)2, –SC(=O)RA, –SC(=O)ORA, –SC(=O)SRA, –SC(=O)N(RA)2, –SC(=NRA)RA, –SC(=NRA)ORA, –SC(=NRA)SRA, –SC(=NRA)N(RA)2, –NRAC(=O)RA, –NRAC(=O)ORA, –NRAC(=O)SRA, –NRAC(=O)N(RA)2, –NRAC(=NRA)RA, –NRAC(=NRA)ORA, –NRAC(=NRA)SRA, –NRAC(=NRA)N(RA)2, –NRAS(=O)RA, –NRAS(=O)ORA, –NRAS(=O)SRA, –NRAS(=O)N(RA)2, –NRAS(=O)2RA, –NRAS(=O)2ORA, –NRAS(=O)2SRA, –NRAS(=O)2N(RA)2, –Si(RA)3, –Si(RA)2ORA, –Si(RA)(ORA)2, –Si(ORA)3, –OSi(RA)3, –OSi(RA)2ORA, –OSi(RA)(ORA)2, –OSi(ORA)3, –B(ORA)2, =O, and / or =S; wherein each occurrence of RAis independently hydrogen, optionally substituted alkyl, optionally substituted alkenyl, optionally substituted alkynyl, optionally substituted heteroalkyl, optionally substituted heteroalkenyl, optionally substituted heteroalkynyl, optionally substituted carbocyclyl, optionally substituted heterocyclyl, optionally substituted aryl, optionally substituted heteroaryl, a nitrogen protecting #13447332v2 group when attached to a nitrogen atom, an oxygen protecting group when attached to an oxygen atom, or a sulfur protecting group when attached to a sulfur atom, or two occurrences of RAare joined together with their intervening atom(s) to form an optionally substituted heterocyclic ring or optionally substituted heteroaryl ring. In some embodiments, L is substituted C12 alkylene, substituted C11 alkylene, substituted C10alkylene, substituted C9alkylene, substituted C8alkylene, substituted C7alkylene, substituted C6 alkylene, substituted C5 alkylene, substituted C4 alkylene, substituted C3 alkylene, substituted C2 alkylene, or substituted C1 alkylene. In some embodiments, L is substituted C12 alkylene. In some embodiments, L is substituted C11alkylene. In some embodiments, L is substituted C10 alkylene. In some embodiments, L is substituted C9 alkylene. In some embodiments, L is substituted C8 alkylene. In some embodiments, L is substituted C7 alkylene. In some embodiments, L is substituted C6alkylene. In some embodiments, L is substituted C5alkylene. In some embodiments, L is substituted C4alkylene. In some embodiments, L is substituted C3 alkylene. In some embodiments, L is substituted C2 alkylene. In some embodiments, L is substituted C1 alkylene. In some embodiments, L is unsubstituted alkylene. In some embodiments, L is unsubstituted C1-12 alkylene. In some embodiments, L is unsubstituted C1-6 alkylene. In some embodiments, L is unsubstituted C1-3 alkylene. In some embodiments, L is unsubstituted C12 alkylene, unsubstituted C11alkylene, unsubstituted C10alkylene, unsubstituted C9alkylene, unsubstituted C8 alkylene, unsubstituted C7 alkylene, unsubstituted C6 alkylene, unsubstituted C5 alkylene, unsubstituted C4 alkylene, unsubstituted C3 alkylene, unsubstituted C2 alkylene, or unsubstituted C1alkylene. In some embodiments, L is unsubstituted C12alkylene. In some embodiments, L is unsubstituted C11alkylene. In some embodiments, L is unsubstituted C10alkylene. In some embodiments, L is unsubstituted C9 alkylene. In some embodiments, L is unsubstituted C8 alkylene. In some embodiments, L is unsubstituted C7 alkylene. In some embodiments, L is unsubstituted C6alkylene. In some embodiments, L is unsubstituted C5alkylene. In some embodiments, L is unsubstituted C4 alkylene. In some embodiments, L is unsubstituted C3 alkylene. In some embodiments, L is unsubstituted C2 alkylene. In some embodiments, L is unsubstituted C1alkylene. In some embodiments, L is methylene, ethylene, n-propylene, isopropylene, n-butylene, tert-butylene, sec-butylene, isobutylene, n-pentylene, 3- pentanylene, amylene, neopentylene, 3-methylene-2-butanylene, tert-amylene, or n-hexylene. In some embodiments, L is methylene, ethylene, n-propylene, n-butylene, n-pentylene, or n- hexylene. In some embodiments, L is methylene. In some embodiments, L is ethylene. In some embodiments, L is n-propylene. In some embodiments, L is n-butylene. In some embodiments, L is n-pentylene. In some embodiments, L is n-hexylene. #13447332v2 In some embodiments, L is optionally substituted heteroalkylene. In some embodiments, L is optionally substituted C1-12heteroalkylene. In some embodiments, L is optionally substituted C1-6heteroalkylene. In some embodiments, L is optionally substituted C1-3heteroalkylene. In some embodiments, L is optionally substituted heteroalkylene containing at least one instance of –O–. In some embodiments, L is optionally substituted heteroalkylene containing at least 1, 2, 3, 4, or 5 instances of . In some embodiments, L is optionally substituted heteroalkylene containing at least one instance of . In some embodiments, L is optionally containing at least one instance of –NRN–, wherein each instance of RNis independently hydrogen, optionally substituted alkyl, optionally substituted alkenyl, optionally substituted alkynyl, optionally substituted heteroalkyl, optionally substituted heteroalkenyl, optionally substituted heteroalkynyl, optionally substituted carbocyclyl, optionally substituted heterocyclyl, optionally substituted aryl, optionally substituted heteroaryl, or a nitrogen protecting group, or two occurrences of RNare joined together with their intervening atoms to form an optionally substituted heterocyclic ring or optionally substituted heteroaryl ring. In some embodiments, L is optionally substituted heteroalkylene containing at least 1 instance of –NH–. In some embodiments, L is optionally substituted heteroalkylene containing at least 1 instance of – N(optionally substituted alkyl)–. In some embodiments, L is optionally substituted heteroalkylene containing at least 1 instance of –N(nitrogen protecting group)–. In some embodiments, the crosslinked protein matrix comprises a moiety of Formula (I- a): wherein each instance of Z is protein matrix. In some embodiments, the crosslinked protein matrix comprises a moiety of Formula (I-a), wherein at least one instance of Z is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the crosslinked protein matrix comprises a moiety of Formula (I-a), wherein at least one instance of Z is bovine serum albumin. In some embodiments, the crosslinked protein matrix comprises a moiety of Formula (I-a), wherein at least one instance of Z is alpha-1-acid glycoprotein. In some embodiments, the crosslinked protein matrix comprises a moiety of Formula (I-a), wherein each instance of Z is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the crosslinked protein matrix comprises a moiety of Formula (I-a), #13447332v2 wherein each instance of Z is bovine serum albumin. In some embodiments, the crosslinked protein matrix comprises a moiety of Formula (I-a), wherein each instance of Z is alpha-1-acid glycoprotein. In some embodiments, the crosslinked protein matrix is prepared by reacting a protein with a crosslinking agent. In some embodiments, the protein is not treated with ethanol prior to reacting with the crosslinking agent. In some embodiments, the protein is not denatured prior to reacting with the crosslinking agent. In some embodiments, the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the protein is bovine serum albumin. In some embodiments, the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent (e.g., bupivacaine) is capable of binding to the protein. In some embodiments, the therapeutic agent (e.g., bupivacaine) is capable of binding to bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent (e.g., bupivacaine) is capable of binding to bovine serum albumin. In some embodiments, the therapeutic agent (e.g., bupivacaine) is capable of binding to alpha-1-acid glycoprotein. Crosslinking Agent In some embodiments, the crosslinking agent comprises at least two acyl groups. In some embodiments, the crosslinking agent comprises two acyl groups. In some embodiments, the crosslinking agent comprises at least two aldehyde groups. In some embodiments, the crosslinking agent comprises two aldehyde groups. In some embodiments, the crosslinking agent is glutaraldehyde. In some embodiments, the crosslinking agent comprises at least two ketone groups. In some embodiments, the crosslinking agent comprises two ketone groups. In some embodiments, the crosslinking agent is of Formula (II): (II), wherein L is optionally substituted alkylene or optionally substituted heteroalkylene. In some embodiments, L is optionally substituted alkylene. In some embodiments, L is optionally substituted C1-12 alkylene. In some embodiments, L is optionally substituted C1-6 alkylene. In some embodiments, L is optionally substituted C1-3alkylene. In some embodiments, L is optionally substituted C12alkylene, optionally substituted C11alkylene, optionally substituted C10 alkylene, optionally substituted C9 alkylene, optionally substituted C8alkylene, optionally substituted C7alkylene, optionally substituted C6alkylene, optionally substituted C5alkylene, optionally substituted C4alkylene, optionally substituted C3alkylene, optionally substituted C2 alkylene, or optionally substituted C1 alkylene. In some embodiments, L is optionally substituted C12alkylene. In some embodiments, L is optionally #13447332v2 substituted C11 alkylene. In some embodiments, L is optionally substituted C10 alkylene. In some embodiments, L is optionally substituted C9alkylene. In some embodiments, L is optionally substituted C8alkylene. In some embodiments, L is optionally substituted C7alkylene. In some embodiments, L is optionally substituted C6 alkylene. In some embodiments, L is optionally substituted C5 alkylene. In some embodiments, L is optionally substituted C4 alkylene. In some embodiments, L is optionally substituted C3alkylene. In some embodiments, L is optionally substituted C2 alkylene. In some embodiments, L is optionally substituted C1 alkylene. In some embodiments, L is substituted alkylene. In some embodiments, L is substituted C1-12alkylene. In some embodiments, L is substituted C1-6alkylene. In some embodiments, L is substituted C1-3 alkylene. In some embodiments, L is alkylene (e.g., C1-12 alkylene, C1-6 alkylene, C1-3 alkylene) substituted with halogen, optionally substituted alkyl, optionally substituted alkenyl, optionally substituted alkynyl, optionally substituted heteroalkyl, optionally substituted heteroalkenyl, optionally substituted heteroalkynyl, optionally substituted carbocyclyl, optionally substituted heterocyclyl, optionally substituted aryl, optionally substituted heteroaryl, –CN, –ORA, –SCN, –SRA, –SSRA, –N3, –NO, –N(RA)2, –NO2, –C(=O)RA, –C(=O)ORA, –C(=O)SRA, –C(=O)N(RA)2, –C(=NRA)RA, –C(=NRA)ORA, –C(=NRA)SRA, –C(=NRA)N(RA)2, –S(=O)RA, –S(=O)ORA, –S(=O)SRA, –S(=O)N(RA)2, –S(=O)2RA, –S(=O)2ORA, –S(=O)2SRA, –S(=O)2N(RA)2, –OC(=O)RA, –OC(=O)ORA, –OC(=O)SRA, –OC(=O)N(RA)2, –OC(=NRA)RA, –OC(=NRA)ORA, –OC(=NRA)SRA, –OC(=NRA)N(RA)2, –OS(=O)RA, –OS(=O)ORA, –OS(=O)SRA, –OS(=O)N(RA)2, –OS(=O)2RA, –OS(=O)2ORA, –OS(=O)2SRA, –OS(=O)2N(RA)2, –ON(RA)2, –SC(=O)RA, –SC(=O)ORA, –SC(=O)SRA, –SC(=O)N(RA)2, –SC(=NRA)RA, –SC(=NRA)ORA, –SC(=NRA)SRA, –SC(=NRA)N(RA)2, –NRAC(=O)RA, –NRAC(=O)ORA, –NRAC(=O)SRA, –NRAC(=O)N(RA)2, –NRAC(=NRA)RA, –NRAC(=NRA)ORA, –NRAC(=NRA)SRA, –NRAC(=NRA)N(RA)2, –NRAS(=O)RA, –NRAS(=O)ORA, –NRAS(=O)SRA, –NRAS(=O)N(RA)2, –NRAS(=O)2RA, –NRAS(=O)2ORA, –NRAS(=O)2SRA, –NRAS(=O)2N(RA)2, –Si(RA)3, –Si(RA)2ORA, –Si(RA)(ORA)2, –Si(ORA)3, –OSi(RA)3, –OSi(RA)2ORA, –OSi(RA)(ORA)2, –OSi(ORA)3, –B(ORA)2, =O, and / or =S; wherein each occurrence of RAis independently hydrogen, optionally substituted alkyl, optionally substituted alkenyl, optionally substituted alkynyl, optionally substituted heteroalkyl, optionally substituted heteroalkenyl, optionally substituted heteroalkynyl, optionally substituted carbocyclyl, optionally substituted heterocyclyl, optionally substituted aryl, optionally substituted heteroaryl, a nitrogen protecting group when attached to a nitrogen atom, an oxygen protecting group when attached to an oxygen atom, or a sulfur protecting group when attached to a sulfur atom, or two occurrences of RAare joined together with their intervening atom(s) to form an optionally substituted heterocyclic ring or optionally substituted heteroaryl ring. #13447332v2 In some embodiments, L is substituted C12 alkylene, substituted C11 alkylene, substituted C10alkylene, substituted C9alkylene, substituted C8alkylene, substituted C7alkylene, substituted C6alkylene, substituted C5alkylene, substituted C4alkylene, substituted C3alkylene, substituted C2 alkylene, or substituted C1 alkylene. In some embodiments, L is substituted C12 alkylene. In some embodiments, L is substituted C11 alkylene. In some embodiments, L is substituted C10alkylene. In some embodiments, L is substituted C9alkylene. In some embodiments, L is substituted C8 alkylene. In some embodiments, L is substituted C7 alkylene. In some embodiments, L is substituted C6 alkylene. In some embodiments, L is substituted C5 alkylene. In some embodiments, L is substituted C4alkylene. In some embodiments, L is substituted C3 alkylene. In some embodiments, L is substituted C2 alkylene. In some embodiments, L is substituted C1 alkylene. In some embodiments, L is unsubstituted alkylene. In some embodiments, L is unsubstituted C1-12alkylene. In some embodiments, L is unsubstituted C1-6alkylene. In some embodiments, L is unsubstituted C1-3 alkylene. In some embodiments, L is unsubstituted C12 alkylene, unsubstituted C11 alkylene, unsubstituted C10 alkylene, unsubstituted C9 alkylene, unsubstituted C8alkylene, unsubstituted C7alkylene, unsubstituted C6alkylene, unsubstituted C5alkylene, unsubstituted C4 alkylene, unsubstituted C3 alkylene, unsubstituted C2 alkylene, or unsubstituted C1 alkylene. In some embodiments, L is unsubstituted C12 alkylene. In some embodiments, L is unsubstituted C11alkylene. In some embodiments, L is unsubstituted C10alkylene. In some embodiments, L is unsubstituted C9 alkylene. In some embodiments, L is unsubstituted C8 alkylene. In some embodiments, L is unsubstituted C7 alkylene. In some embodiments, L is unsubstituted C6alkylene. In some embodiments, L is unsubstituted C5alkylene. In some embodiments, L is unsubstituted C4alkylene. In some embodiments, L is unsubstituted C3 alkylene. In some embodiments, L is unsubstituted C2 alkylene. In some embodiments, L is unsubstituted C1 alkylene. In some embodiments, L is methylene, ethylene, n-propylene, isopropylene, n-butylene, tert-butylene, sec-butylene, isobutylene, n-pentylene, 3- pentanylene, amylene, neopentylene, 3-methylene-2-butanylene, tert-amylene, or n-hexylene. In some embodiments, L is methylene, ethylene, n-propylene, n-butylene, n-pentylene, or n- hexylene. In some embodiments, L is methylene. In some embodiments, L is ethylene. In some embodiments, L is n-propylene. In some embodiments, L is n-butylene. In some embodiments, L is n-pentylene. In some embodiments, L is n-hexylene. In some embodiments, L is optionally substituted heteroalkylene. In some embodiments, L is optionally substituted C1-12heteroalkylene. In some embodiments, L is optionally substituted C1-6 heteroalkylene. In some embodiments, L is optionally substituted C1-3 heteroalkylene. #13447332v2 In some embodiments, L is optionally substituted heteroalkylene containing at least one instance of –O–. In some embodiments, L is optionally substituted heteroalkylene containing at least 1, 2, 3, 4, or 5 instances of . In some embodiments, L is optionally substituted heteroalkylene containing at least one instance of . In some embodiments, L is optionally substituted heteroalkylene containing at least one instance of –NRN–, wherein each instance of RNis independently hydrogen, optionally substituted alkyl, optionally substituted alkenyl, optionally substituted alkynyl, optionally substituted heteroalkyl, optionally substituted heteroalkenyl, optionally substituted heteroalkynyl, optionally substituted carbocyclyl, optionally substituted heterocyclyl, optionally substituted aryl, optionally substituted heteroaryl, or a nitrogen protecting group, or two occurrences of RNare joined together with their intervening atoms to form an optionally substituted heterocyclic ring or optionally substituted heteroaryl ring. In some embodiments, L is optionally substituted heteroalkylene containing at least 1 instance of –NH–. In some embodiments, L is optionally substituted heteroalkylene containing at least 1 instance of – N(optionally substituted alkyl)–. In some embodiments, L is optionally substituted heteroalkylene containing at least 1 instance of –N(nitrogen protecting group)–. Additional Embodiments In some embodiments, bovine serum albumin (BSA) refers to a compound having CAS Registry Number 9048-46-8. In some embodiments, BSA is encoded by the bovine ALB gene, located on chromosome 6 (e.g., encoded by Ensembl ID NO: ENSBTAG00000017121, Chromosome 6: 88,484,961-88,503,334 forward strand). In some embodiments, ALB encodes a peptide that is represented by NCBI Reference Sequence NP_851335.1. In some embodiments, ALB encodes an mRNA comprising the sequence set forth in NCBI Reference Sequence NM_180992.2. In some embodiments, alpha-1-acid glycoprotein refers to a compound having CAS Registry Number 66455-27-4. In some embodiments, alpha-1-acid glycoprotein is encoded by the human ORM1 gene, located on chromosome 9 (e.g., encoded by Ensembl ID NO: ENSG00000229314, Chromosome 9: 114,323,098-114,326,479 forward strand). In some embodiments, ORM1 encodes a peptide that is represented by NCBI Reference Sequence NP_000598.2. In some embodiments, ORM1 encodes an mRNA comprising the sequence set forth in NCBI Reference Sequence NM_000607.4. In some embodiments, the bovine serum albumin is present in a concentration of between about 25 mg / mL and about 500 mg / mL, between about 25 mg / mL and about 250 #13447332v2 mg / mL, between about 25 mg / mL and about 200 mg / mL, between about 25 mg / mL and about 175 mg / mL, between about 25 mg / mL and about 150 mg / mL, between about 25 mg / mL and about 125 mg / mL, between about 25 mg / mL and about 112.5 mg / mL, between about 25 mg / mL and about 105 mg / mL, between about 25 mg / mL and about 100 mg / mL, between about 37.5 mg / mL and about 500 mg / mL, between about 37.5 mg / mL and about 250 mg / mL, between about 37.5 mg / mL and about 200 mg / mL, between about 37.5 mg / mL and about 175 mg / mL, between about 37.5 mg / mL and about 150 mg / mL, between about 37.5 mg / mL and about 125 mg / mL, between about 37.5 mg / mL and about 112.5 mg / mL, between about 37.5 mg / mL and about 105 mg / mL, between about 37.5 mg / mL and about 100 mg / mL, between about 45 mg / mL and about 500 mg / mL, between about 45 mg / mL and about 250 mg / mL, between about 45 mg / mL and about 200 mg / mL, between about 45 mg / mL and about 175 mg / mL, between about 45 mg / mL and about 150 mg / mL, between about 45 mg / mL and about 125 mg / mL, between about 45 mg / mL and about 112.5 mg / mL, between about 45 mg / mL and about 105 mg / mL, between about 45 mg / mL and about 100 mg / mL, between about 50 mg / mL and about 500 mg / mL, between about 50 mg / mL and about 250 mg / mL, between about 50 mg / mL and about 200 mg / mL, between about 50 mg / mL and about 175 mg / mL, between about 50 mg / mL and about 150 mg / mL, between about 50 mg / mL and about 125 mg / mL, between about 50 mg / mL and about 112.5 mg / mL, between about 50 mg / mL and about 105 mg / mL, or between about 50 mg / mL and about 100 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 25 mg / mL and about 500 mg / mL, between about 25 mg / mL and about 250 mg / mL, between about 25 mg / mL and about 200 mg / mL, between about 25 mg / mL and about 175 mg / mL, between about 25 mg / mL and about 150 mg / mL, between about 25 mg / mL and about 125 mg / mL, between about 25 mg / mL and about 112.5 mg / mL, between about 25 mg / mL and about 105 mg / mL, between about 25 mg / mL and about 100 mg / mL, between about 37.5 mg / mL and about 125 mg / mL, between about 37.5 mg / mL and about 112.5 mg / mL, between about 37.5 mg / mL and about 105 mg / mL, between about 37.5 mg / mL and about 100 mg / mL, between about 45 mg / mL and about 125 mg / mL, between about 45 mg / mL and about 112.5 mg / mL, between about 45 mg / mL and about 105 mg / mL, between about 45 mg / mL and about 100 mg / mL, between about 50 mg / mL and about 125 mg / mL, between about 50 mg / mL and about 112.5 mg / mL, between about 50 mg / mL and about 105 mg / mL, or between about 50 mg / mL and about 100 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 25 mg / mL and about 125 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 37.5 mg / mL and about 112.5 mg / mL. In #13447332v2 some embodiments, the bovine serum albumin is present in a concentration of between about 45 mg / mL and about 105 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 50 mg / mL and about 100 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 25 mg / mL, about 30 mg / mL, about 35 mg / mL, about 37.5 mg / mL, about 40 mg / mL, about 42.5 mg / mL, about 45 mg / mL, about 47.5 mg / mL, about 48 mg / mL, about 49 mg / mL, about 50 mg / mL, about 51 mg / mL, about 52 mg / mL, about 52.5 mg / mL, about 55 mg / mL, about 57.5 mg / mL, about 60 mg / mL, about 62.5 mg / mL, about 65 mg / mL, about 70 mg / mL, about 75 mg / mL, about 80 mg / mL about 85 mg / mL, about 87.5 mg / mL, about 90 mg / mL, about 92.5 mg / mL, about 95 mg / mL, about 97.5 mg / mL, about 98 mg / mL, about 99 mg / mL, about 100 mg / mL, about 101 mg / mL, about 102 mg / mL, about 102.5 mg / mL, about 105 mg / mL, about 107.5 mg / mL, about 110 mg / mL, about 112.5 mg / mL, about 115 mg / mL, about 120 mg / mL, about 125 mg / mL, about 130 mg / mL, about 135 mg / mL, about 140 mg / mL, about 145 mg / mL, about 150 mg / mL, about 155 mg / mL, about 160 mg / mL, about 165 mg / mL, about 170 mg / mL, about 175 mg / mL, about 200 mg / mL, about 225 mg / mL, about 250 mg / mL, about 275 mg / mL, about 300 mg / mL, about 350 mg / mL, about 400 mg / mL, or about 500 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 35 mg / mL, about 37.5 mg / mL, about 40 mg / mL, about 42.5 mg / mL, about 45 mg / mL, about 47.5 mg / mL, about 48 mg / mL, about 49 mg / mL, about 50 mg / mL, about 51 mg / mL, about 52 mg / mL, about 52.5 mg / mL, about 55 mg / mL, about 57.5 mg / mL, about 60 mg / mL, about 62.5 mg / mL, or about 65 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 35 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 37.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 40 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 42.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 45 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 47.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 48 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 49 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 50 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 51 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 52 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 52.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about #13447332v2 55 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 57.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 60 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 62.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 65 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 85 mg / mL, about 87.5 mg / mL, about 90 mg / mL, about 92.5 mg / mL, about 95 mg / mL, about 97.5 mg / mL, about 98 mg / mL, about 99 mg / mL, about 100 mg / mL, about 101 mg / mL, about 102 mg / mL, about 102.5 mg / mL, about 105 mg / mL, about 107.5 mg / mL, about 110 mg / mL, about 112.5 mg / mL, or about 115 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 85 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 87.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 90 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 92.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 95 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 97.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 98 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 99 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 100 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 101 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 102 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 102.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 105 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 107.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 110 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 112.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 115 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of between about 1 mg / mL and about 25 mg / mL, between about 1 mg / mL and about 20 mg / mL, between about 1 mg / mL and about 15 mg / mL, between about 1 mg / mL and about 14 mg / mL, between about 1 mg / mL and about 13 mg / mL, between about 1 mg / mL and about 12.5 mg / mL, between about 1 mg / mL and about 12 mg / mL, between about 1 mg / mL and about 11.5 mg / mL, between about 1 mg / mL and about 11 mg / mL, between about 1 mg / mL and about 10.5 mg / mL, between about 1 mg / mL and about 10 mg / mL, between about 2.5 mg / mL and about 25 mg / mL, between about #13447332v2 2.5 mg / mL and about 20 mg / mL, between about 2.5 mg / mL and about 15 mg / mL, between about 2.5 mg / mL and about 14 mg / mL, between about 2.5 mg / mL and about 13 mg / mL, between about 2.5 mg / mL and about 12.5 mg / mL, between about 2.5 mg / mL and about 12 mg / mL, between about 2.5 mg / mL and about 11.5 mg / mL, between about 2.5 mg / mL and about 11 mg / mL, between about 2.5 mg / mL and about 10.5 mg / mL, between about 2.5 mg / mL and about 10 mg / mL, between about 3 mg / mL and about 25 mg / mL, between about 3 mg / mL and about 20 mg / mL, between about 3 mg / mL and about 15 mg / mL, between about 3 mg / mL and about 14 mg / mL, between about 3 mg / mL and about 13 mg / mL, between about 3 mg / mL and about 12.5 mg / mL, between about 3 mg / mL and about 12 mg / mL, between about 3 mg / mL and about 11.5 mg / mL, between about 3 mg / mL and about 11 mg / mL, between about 3 mg / mL and about 10.5 mg / mL, between about 3 mg / mL and about 10 mg / mL, between about 3.5 mg / mL and about 25 mg / mL, between about 3.5 mg / mL and about 20 mg / mL, between about 3.5 mg / mL and about 15 mg / mL, between about 3.5 mg / mL and about 14 mg / mL, between about 3.5 mg / mL and about 13 mg / mL, between about 3.5 mg / mL and about 12.5 mg / mL, between about 3.5 mg / mL and about 12 mg / mL, between about 3.5 mg / mL and about 11.5 mg / mL, between about 3.5 mg / mL and about 11 mg / mL, between about 3.5 mg / mL and about 10.5 mg / mL, between about 3.5 mg / mL and about 10 mg / mL, between about 4 mg / mL and about 25 mg / mL, between about 4 mg / mL and about 20 mg / mL, between about 4 mg / mL and about 15 mg / mL, between about 4 mg / mL and about 14 mg / mL, between about 4 mg / mL and about 13 mg / mL, between about 4 mg / mL and about 12.5 mg / mL, between about 4 mg / mL and about 12 mg / mL, between about 4 mg / mL and about 11.5 mg / mL, between about 4 mg / mL and about 11 mg / mL, between about 4 mg / mL and about 10.5 mg / mL, between about 4 mg / mL and about 10 mg / mL, between about 4.5 mg / mL and about 25 mg / mL, between about 4.5 mg / mL and about 20 mg / mL, between about 4.5 mg / mL and about 15 mg / mL, between about 4.5 mg / mL and about 14 mg / mL, between about 4.5 mg / mL and about 13 mg / mL, between about 4.5 mg / mL and about 12.5 mg / mL, between about 4.5 mg / mL and about 12 mg / mL, between about 4.5 mg / mL and about 11.5 mg / mL, between about 4.5 mg / mL and about 11 mg / mL, between about 4.5 mg / mL and about 10.5 mg / mL, between about 4.5 mg / mL and about 10 mg / mL, between about 5 mg / mL and about 25 mg / mL, between about 5 mg / mL and about 20 mg / mL, between about 5 mg / mL and about 15 mg / mL, between about 5 mg / mL and about 14 mg / mL, between about 5 mg / mL and about 13 mg / mL, between about 5 mg / mL and about 12.5 mg / mL, between about 5 mg / mL and about 12 mg / mL, between about 5 mg / mL and about 11.5 mg / mL, between about 5 mg / mL and about 11 mg / mL, between about 5 mg / mL and about 10.5 mg / mL, or between about 5 mg / mL and about 10 mg / mL. #13447332v2 In some embodiments, the glutaraldehyde is present in a concentration of between about 1 mg / mL and about 15 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of between about 2.5 mg / mL and about 12.5 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of between about 4 mg / mL and about 11 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of between about 4.5 mg / mL and about 10.5 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of between about 5 mg / mL and about 10 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 1 mg / mL, about 1.5 mg / mL, about 2 mg / mL, about 2.5 mg / mL, about 3 mg / mL, about 3.5 mg / mL, about 4 mg / mL, about 4.5 mg / mL, about 5 mg / mL, about 5.5 mg / mL, about 6 mg / mL, about 6.5 mg / mL, about 7 mg / mL, about 7.5 mg / mL, about 8 mg / mL, about 8.5 mg / mL, about 9 mg / mL, about 9.5 mg / mL, about 10 mg / mL, about 10.5 mg / mL, about 11 mg / mL, about 11.5 mg / mL, about 12 mg / mL, about 12.5 mg / mL, about 13 mg / mL, about 13.5 mg / mL, about 14 mg / mL, about 14.5 mg / mL, about 15 mg / mL, about 16 mg / mL, about 17 mg / mL, about 18 mg / mL, about 19 mg / mL, about 20 mg / mL, about 21 mg / mL, about 22 mg / mL, about 23 mg / mL, about 24 mg / mL, or about 25 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 1 mg / mL, about 2.5 mg / mL, about 4 mg / mL, about 4.5 mg / mL, about 5 mg / mL, about 5.5 mg / mL, about 6 mg / mL, about 7.5 mg / mL, about 9 mg / mL, about 9.5 mg / mL, about 10 mg / mL, about 10.5 mg / mL, about 11 mg / mL, about 12.5 mg / mL, or about 15 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 1 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 2.5 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 7.5 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 12.5 mg / mL. In some embodiments, the glutaraldehyde is present in a concentration of about 15 mg / mL. #13447332v2 In some embodiments, the bovine serum albumin is present in a concentration of between about 25 mg / mL and about 125 mg / mL, and the glutaraldehyde is present in a concentration of between about 1 mg / mL and about 15 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 25 mg / mL and about 125 mg / mL, and the glutaraldehyde is present in a concentration of between about 2.5 mg / mL and about 12.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 25 mg / mL and about 125 mg / mL, and the glutaraldehyde is present in a concentration of between about 4 mg / mL and about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 25 mg / mL and about 125 mg / mL, and the glutaraldehyde is present in a concentration of between about 4.5 mg / mL and about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 25 mg / mL and about 125 mg / mL, and the glutaraldehyde is present in a concentration of between about 5 mg / mL and about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 37.5 mg / mL and about 112.5 mg / mL, and the glutaraldehyde is present in a concentration of between about 1 mg / mL and about 15 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 37.5 mg / mL and about 112.5 mg / mL, and the glutaraldehyde is present in a concentration of between about 2.5 mg / mL and about 12.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 37.5 mg / mL and about 112.5 mg / mL, and the glutaraldehyde is present in a concentration of between about 4 mg / mL and about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 37.5 mg / mL and about 112.5 mg / mL, and the glutaraldehyde is present in a concentration of between about 4.5 mg / mL and about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 37.5 mg / mL and about 112.5 mg / mL, and the glutaraldehyde is present in a concentration of between about 5 mg / mL and about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 45 mg / mL and about 105 mg / mL, and the glutaraldehyde is present in a concentration of between about 1 mg / mL and about 15 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 45 mg / mL and about 105 mg / mL, and the glutaraldehyde is present in a concentration of between about 2.5 mg / mL and about 12.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 45 mg / mL and about 105 mg / mL, and the glutaraldehyde is present in a concentration of between about 4 mg / mL and about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 45 #13447332v2 mg / mL and about 105 mg / mL, and the glutaraldehyde is present in a concentration of between about 4.5 mg / mL and about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 45 mg / mL and about 105 mg / mL, and the glutaraldehyde is present in a concentration of between about 5 mg / mL and about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 50 mg / mL and about 100 mg / mL, and the glutaraldehyde is present in a concentration of between about 1 mg / mL and about 15 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 50 mg / mL and about 100 mg / mL, and the glutaraldehyde is present in a concentration of between about 2.5 mg / mL and about 12.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 50 mg / mL and about 100 mg / mL, and the glutaraldehyde is present in a concentration of between about 4 mg / mL and about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 50 mg / mL and about 100 mg / mL, and the glutaraldehyde is present in a concentration of between about 4.5 mg / mL and about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of between about 50 mg / mL and about 100 mg / mL, and the glutaraldehyde is present in a concentration of between about 5 mg / mL and about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 40 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 40 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 40 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 40 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 40 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 40 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 40 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 40 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 40 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum #13447332v2 albumin is present in a concentration of about 40 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 45 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 45 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 45 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 45 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 45 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 45 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 45 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 45 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 45 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 45 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 47.5 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 47.5 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 47.5 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 47.5 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 47.5 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 47.5 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 47.5 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 47.5 mg / mL, and #13447332v2 the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 47.5 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 47.5 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 49 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 49 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 49 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 49 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 49 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 49 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 49 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 49 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 49 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 49 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In #13447332v2 some embodiments, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 51 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 51 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 51 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 51 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 51 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 51 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 51 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 51 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 51 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 51 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 52.5 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 52.5 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 52.5 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 52.5 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present #13447332v2 in a concentration of about 52.5 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 52.5 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 52.5 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 52.5 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 52.5 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 52.5 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 55 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 55 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 55 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 55 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 55 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 55 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 55 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 55 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 55 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 55 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 60 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 60 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 60 mg / mL, and the glutaraldehyde #13447332v2 is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 60 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 60 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 60 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 60 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 60 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 60 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 60 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 90 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 90 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 90 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 90 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 90 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 90 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 90 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 90 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 90 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 90 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 95 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some #13447332v2 embodiments, the bovine serum albumin is present in a concentration of about 95 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 95 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 95 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 95 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 95 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 95 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 95 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 95 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 95 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 97.5 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 97.5 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 97.5 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 97.5 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 97.5 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 97.5 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 97.5 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 97.5 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 97.5 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum #13447332v2 albumin is present in a concentration of about 97.5 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 102.5 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 102.5 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 102.5 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 102.5 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 102.5 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 102.5 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 102.5 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the #13447332v2 bovine serum albumin is present in a concentration of about 102.5 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 102.5 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 102.5 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 105 mg / mL, and the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 105 mg / mL, and the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 105 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 105 mg / mL, and the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 105 mg / mL, and the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 105 mg / mL, and the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 105 mg / mL, and the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 105 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 105 mg / mL, and the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 105 mg / mL, and the glutaraldehyde is present in a concentration of about 11 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 110 mg / mL. the glutaraldehyde is present in a concentration of about 4 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 110 mg / mL. the glutaraldehyde is present in a concentration of about 4.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 110 mg / mL. the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 110 mg / mL. the glutaraldehyde is present in a concentration of about 5.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 110 mg / mL. the glutaraldehyde is present in a concentration of about 6 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of #13447332v2 about 110 mg / mL. the glutaraldehyde is present in a concentration of about 9 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 110 mg / mL. the glutaraldehyde is present in a concentration of about 9.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 110 mg / mL. the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 110 mg / mL. the glutaraldehyde is present in a concentration of about 10.5 mg / mL. In some embodiments, the bovine serum albumin is present in a concentration of about 110 mg / mL. the glutaraldehyde is present in a concentration of about 11 mg / mL. Nanoparticle As described herein, the nanoparticle comprises a therapeutic agent or a diagnostic agent; and the nanoparticle is embedded in the crosslinked protein matrix. In some embodiments, the nanoparticle consists of a therapeutic agent or a diagnostic agent, and the nanoparticle is embedded in the crosslinked protein matrix. In some embodiments, the nanoparticle consists essentially of a therapeutic agent or a diagnostic agent, and the nanoparticle is embedded in the crosslinked protein matrix. In some embodiments, the nanoparticle does not comprise a protein. In some embodiments, the nanoparticle does not comprise a crosslinked protein. In some embodiments, the nanoparticle does not comprise the crosslinked protein matrix. In some embodiments, the nanoparticle does not comprise the hydrogel. In some embodiments, the nanoparticle does not comprise water. In some embodiments, the nanoparticle does not comprise bovine serum albumin. In some embodiments, the nanoparticle does not comprise a crosslinking agent. In some embodiments, the nanoparticle does not comprise glutaraldehyde. In some embodiments, the nanoparticle comprises a hydrodynamic diameter of between about 100 nm and about 400 nm, between about 100 nm and about 300 nm, between about 100 nm and about 200 nm, between about 200 nm and about 300 nm, between about 125 nm and about 300 nm, between about 125 nm and about 275 nm, between about 125 nm and about 250 nm, between about 125 nm and about 225 nm, between about 150 nm and about 300 nm, between about 150 nm and about 275 nm, between about 150 nm and about 250 nm, between about 150 nm and about 225 nm, between about 175 nm and about 300 nm, between about 175 nm and about 275 nm, between about 175 nm and about 250 nm, or between about 175 nm and about 225 nm. In some embodiments, the nanoparticle comprises a hydrodynamic diameter of about 100 nm, about 110 nm, about 120 nm, about 130 nm, about 140 nm, about 150 nm, about 160 #13447332v2 nm, about 170 nm, about 175 nm, about 180 nm, about 185 nm, about 190 nm, about 195 nm, about 200 nm, about 205 nm, about 210 nm, about 215 nm, about 220 nm, about 225 nm, about 230 nm, about 240 nm, about 250 nm, about 260 nm, about 270 nm, about 280 nm, about 290 nm, about 300 nm, about 310 nm, about 320 nm, about 330 nm, about 340 nm, about 350 nm, about 360 nm, about 370 nm, about 380 nm, about 390 nm, or about 400 nm. In some embodiments, the nanoparticle comprises a hydrodynamic diameter of about 175 nm. In some embodiments, the nanoparticle comprises a hydrodynamic diameter of about 180 nm. In some embodiments, the nanoparticle comprises a hydrodynamic diameter of about 185 nm. In some embodiments, the nanoparticle comprises a hydrodynamic diameter of about 190 nm. In some embodiments, the nanoparticle comprises a hydrodynamic diameter of about 195 nm. In some embodiments, the nanoparticle comprises a hydrodynamic diameter of about 200 nm. In some embodiments, the nanoparticle comprises a hydrodynamic diameter of about 205 nm. In some embodiments, the nanoparticle comprises a hydrodynamic diameter of about 210 nm. In some embodiments, the nanoparticle comprises a hydrodynamic diameter of about 215 nm. In some embodiments, the nanoparticle comprises a hydrodynamic diameter of about 220 nm. In some embodiments, the nanoparticle comprises a hydrodynamic diameter of about 225 nm. In some embodiments, the nanoparticle is covalently attached to the hydrogel. In some embodiments, the nanoparticle is not covalently attached to the hydrogel. In some embodiments, the nanoparticle is covalently attached to the crosslinked protein matrix. In some embodiments, the nanoparticle is not covalently attached to the crosslinked protein matrix. In some embodiments, the nanoparticle is not covalently attached to the hydrogel and / or the nanoparticle is not covalently attached to the crosslinked protein matrix. In some embodiments, the nanoparticle is not covalently attached to the hydrogel, and the nanoparticle is not covalently attached to the crosslinked protein matrix. Protein-Stabilized Nanoparticle As described herein, the protein-stabilized nanoparticle comprises a therapeutic agent or a diagnostic agent; and the protein-stabilized nanoparticle is embedded in the crosslinked protein matrix. In some embodiments, the protein-stabilized nanoparticle consists of a therapeutic agent or a diagnostic agent, and the protein-stabilized nanoparticle is embedded in the crosslinked protein matrix. In some embodiments, the protein-stabilized nanoparticle consists essentially of a therapeutic agent or a diagnostic agent, and the protein-stabilized nanoparticle is embedded in the crosslinked protein matrix. #13447332v2 In some embodiments, the protein-stabilized nanoparticle does not comprise a protein. In some embodiments, the protein-stabilized nanoparticle does not comprise a crosslinked protein. In some embodiments, the protein-stabilized nanoparticle does not comprise the crosslinked protein matrix. In some embodiments, the protein-stabilized nanoparticle does not comprise the hydrogel. In some embodiments, the protein-stabilized nanoparticle does not comprise water. In some embodiments, the protein-stabilized nanoparticle does not comprise bovine serum albumin. In some embodiments, the protein-stabilized nanoparticle does not comprise a crosslinking agent. In some embodiments, the protein-stabilized nanoparticle does not comprise glutaraldehyde. In some embodiments, the crosslinked protein matrix comprises a crosslinked protein, and the protein-stabilized nanoparticle comprises a therapeutic agent (e.g., bupivacaine) capable of binding to the crosslinked protein. In some embodiments, the crosslinked protein matrix comprises crosslinked bovine serum albumin or crosslinked alpha-1-acid glycoprotein, and the protein-stabilized nanoparticle comprises a therapeutic agent (e.g., bupivacaine) capable of binding to the crosslinked bovine serum albumin or crosslinked alpha-1-acid glycoprotein. In some embodiments, the crosslinked protein matrix comprises crosslinked bovine serum albumin, and the protein-stabilized nanoparticle comprises a therapeutic agent (e.g., bupivacaine) capable of binding to the crosslinked bovine serum albumin. In some embodiments, the crosslinked protein matrix comprises crosslinked alpha-1-acid glycoprotein, and the protein-stabilized nanoparticle comprises a therapeutic agent (e.g., bupivacaine) capable of binding to the crosslinked alpha-1-acid glycoprotein. In some embodiments, the crosslinked protein matrix is prepared by reacting a protein with a crosslinking agent, and the protein-stabilized nanoparticle comprises a therapeutic agent (e.g., bupivacaine) capable of binding to the protein. In some embodiments, the crosslinked protein matrix is prepared by reacting bovine serum albumin or alpha-1-acid glycoprotein with a crosslinking agent, and the protein-stabilized nanoparticle comprises a therapeutic agent (e.g., bupivacaine) capable of binding to the bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the crosslinked protein matrix is prepared by reacting bovine serum albumin with a crosslinking agent, and the protein-stabilized nanoparticle comprises a therapeutic agent (e.g., bupivacaine) capable of binding to the bovine serum albumin. In some embodiments, the crosslinked protein matrix is prepared by reacting alpha-1-acid glycoprotein with a crosslinking agent, and the protein-stabilized nanoparticle comprises a therapeutic agent (e.g., bupivacaine) capable of binding to the alpha-1-acid glycoprotein. In some embodiments, the protein-stabilized nanoparticle comprises a hydrodynamic diameter of between about 100 nm and about 400 nm, between about 100 nm and about 300 nm, #13447332v2 between about 100 nm and about 200 nm, between about 200 nm and about 300 nm, between about 125 nm and about 300 nm, between about 125 nm and about 275 nm, between about 125 nm and about 250 nm, between about 125 nm and about 225 nm, between about 150 nm and about 300 nm, between about 150 nm and about 275 nm, between about 150 nm and about 250 nm, between about 150 nm and about 225 nm, between about 175 nm and about 300 nm, between about 175 nm and about 275 nm, between about 175 nm and about 250 nm, or between about 175 nm and about 225 nm. In some embodiments, the protein-stabilized nanoparticle comprises a hydrodynamic diameter of about 100 nm, about 110 nm, about 120 nm, about 130 nm, about 140 nm, about 150 nm, about 160 nm, about 170 nm, about 175 nm, about 180 nm, about 185 nm, about 190 nm, about 195 nm, about 200 nm, about 205 nm, about 210 nm, about 215 nm, about 220 nm, about 225 nm, about 230 nm, about 240 nm, about 250 nm, about 260 nm, about 270 nm, about 280 nm, about 290 nm, about 300 nm, about 310 nm, about 320 nm, about 330 nm, about 340 nm, about 350 nm, about 360 nm, about 370 nm, about 380 nm, about 390 nm, or about 400 nm. In some embodiments, the protein-stabilized nanoparticle comprises a hydrodynamic diameter of about 175 nm. In some embodiments, the protein-stabilized nanoparticle comprises a hydrodynamic diameter of about 180 nm. In some embodiments, the protein-stabilized nanoparticle comprises a hydrodynamic diameter of about 185 nm. In some embodiments, the protein-stabilized nanoparticle comprises a hydrodynamic diameter of about 190 nm. In some embodiments, the protein-stabilized nanoparticle comprises a hydrodynamic diameter of about 195 nm. In some embodiments, the protein-stabilized nanoparticle comprises a hydrodynamic diameter of about 200 nm. In some embodiments, the protein-stabilized nanoparticle comprises a hydrodynamic diameter of about 205 nm. In some embodiments, the protein-stabilized nanoparticle comprises a hydrodynamic diameter of about 210 nm. In some embodiments, the protein-stabilized nanoparticle comprises a hydrodynamic diameter of about 215 nm. In some embodiments, the protein-stabilized nanoparticle comprises a hydrodynamic diameter of about 220 nm. In some embodiments, the protein-stabilized nanoparticle comprises a hydrodynamic diameter of about 225 nm. In some embodiments, the protein-stabilized nanoparticle is covalently attached to the hydrogel. In some embodiments, the protein-stabilized nanoparticle is not covalently attached to the hydrogel. In some embodiments, the protein-stabilized nanoparticle is covalently attached to the crosslinked protein matrix. In some embodiments, the protein-stabilized nanoparticle is not covalently attached to the crosslinked protein matrix. In some embodiments, the protein- stabilized nanoparticle is not covalently attached to the hydrogel and / or the protein-stabilized nanoparticle is not covalently attached to the crosslinked protein matrix. In some embodiments, #13447332v2 the protein-stabilized nanoparticle is not covalently attached to the hydrogel, and the protein- stabilized nanoparticle is not covalently attached to the crosslinked protein matrix. Diagnostic Agent In some embodiments, the protein-stabilized nanoparticle comprises a diagnostic agent. In some embodiments, the diagnostic agent is a fluorophore. In some embodiments, the diagnostic agent is a small molecule or a biologic. In some embodiments, the diagnostic agent is a small molecule. In some embodiments, the diagnostic agent is conjugated to a protein, a polymer, or a small molecule. In some embodiments, the diagnostic agent is conjugated to the protein-stabilized nanoparticle. In some embodiments, the diagnostic agent is not conjugated to the protein-stabilized nanoparticle. In some embodiments, the diagnostic agent is Sulforhodamine B, Cy-5.5, indocyanine green, fluorescein isothiocyanate, methylene blue, or coumarin. In some embodiments, the diagnostic agent comprises, by weight, about 0.05% to about 10% of the total mass of the composition. In some embodiments, the diagnostic agent comprises, by weight, about 0.05% to about 0.2%, about 0.1% to about 0.2%, about 0.12% to about 0.2%, about 0.13% to about 0.2%, about 0.14% to about 0.2%, about 0.15% to about 0.2%, about 0.15%, or about 0.16% of the total mass of the composition. In some embodiments, the diagnostic agent comprises, by weight, about 2% to about 4%, about 2.5% to about 3.5%, about 2% to about 3%, about 2.8% to about 3.2%, about 2.8% to about 3.0%, about 2.8%, about 2.9%, about 3.0%, about 3.1%, or about 0.16% of the total mass of the composition. In some embodiments, the amount of the diagnostic agent in the composition is about 1%, about 2%, about 3%, about 4%, about 5%, about 6%, about 7%, about 8%, about 9%, about 10%, about 11%, about 12%, about 13%, about 14%, about 15%, about 16%, about 17%, about 18%, about 19%, about 20%, about 21%, about 22%, about 23%, about 24%, about 25%, about 26%, about 27%, about 28%, about 29%, about 30%, about 40%, about 40%, about 50%, about 60%, about 70%, about 80%, about 90%, or about 100% greater than the amount of the diagnostic agent in a composition that is not a composition disclosed herein. Therapeutic Agent In some embodiments, the nanoparticle comprises a therapeutic agent. In some embodiments, the nanoparticle does not comprise a diagnostic agent. In some embodiments, the protein-stabilized nanoparticle comprises a therapeutic agent. In some embodiments, the protein- stabilized nanoparticle does not comprise a diagnostic agent. In some embodiments, the therapeutic agent is a small molecule or a biologic. In some embodiments, the therapeutic agent is a small molecule, a protein, or a nucleic acid. In some #13447332v2 embodiments, the therapeutic agent is a small molecule. In some embodiments, the therapeutic agent is an anesthetic. In some embodiments, the therapeutic agent is a free base form of an anesthetic. In some embodiments, the therapeutic agent does not comprise a primary or secondary amine. In some embodiments, the therapeutic agent is not doxorubicin. In some embodiments, the therapeutic agent is hydrophobic. In some embodiments, the therapeutic agent is hydrophilic. In some embodiments, the therapeutic agent is amphiphilic. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than 0. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than 0.5. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than 1. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than 1.5. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than 2. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than 2.5. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than 3. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than 3.5. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than 4. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than 4.5. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than 5. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than -0.5. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than -1. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than -1.5. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than -2. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than -2.5. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than -3. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than -3.5. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than -4. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than -4.5. In certain embodiments, the therapeutic agent has a LogD or LogP that is equal to or less than -5. In certain embodiments, the therapeutic agent has a LogD or LogP that is -5 to 0. In certain embodiments, the therapeutic agent has a LogD or LogP that is 0 to 5. In some embodiments, the therapeutic agent is a local anesthetic (e.g., tetrodotoxin, saxitoxin, neosaxitoxin, bupivacaine, amylocaine, ambucaine, articaine, benzocaine, benzonatate, butacaine, butanilicaine, carbocaine, cepastat, chloraseptic, chloroprocaine, cinchocaine, citanest, cyclomethycaine, dibucaine, diperodon, dimethocaine, eucaine, #13447332v2 etidocaine, fomocaine, fotocaine, hydroxyprocaine, isobucaine, levobupivacaine, lidocaine, marcaine, mepivacaine, meprylcaine, metabutoxycaine, nitracaine, orthocaine, orabloc, oxetacaine, oxybuprocaine, paraethoxycaine, phenacaine, piperocaine, piridocaine, polocaine, posimir, pramocaine, prilocaine, primacaine, procaine, procainamide, proparacaine, propoxycaine, pyrrocaine, quinisocaine, ropivacaine, sensorcaine, septocaine, trimecaine, tetracaine, tolycaine, tropacocaine, ulcerease, xylocaine, or zorcaine). In some embodiments, the therapeutic agent is a free base form of a local anesthetic. In some embodiments, the therapeutic agent is a local anesthetic compound, for example, but not limited to, an amino ester compound (e.g., procaine, tetracaine, chloroprocaine, benzocaine, butacaine, dimethocaine) or an amino amide compound (e.g., procainamide, lidocaine). In some embodiments, the local anesthetic is a sodium channel blocker, for example, a site 1 sodium channel blocker (e.g., tetrodotoxin, saxitoxins (saxitoxin, neosaxitoxin), gonyautoxins (gonyautoxin V, gonyautoxin VI), µ- conotoxins)) or an amino amide local anesthetic. In some embodiments, the therapeutic agent is a site 1 sodium channel blocker, amino ester anesthetic, or an amino amide anesthetic, or a derivative thereof. In some embodiments, the therapeutic agent is tetrodotoxin, saxitoxin, neosaxitoxin, bupivacaine, amylocaine, ambucaine, articaine, benzocaine, benzonatate, butacaine, butanilicaine, carbocaine, cepastat, chloraseptic, chloroprocaine, cinchocaine, citanest, cyclomethycaine, dibucaine, diperodon, dimethocaine, eucaine, etidocaine, fomocaine, fotocaine, hydroxyprocaine, isobucaine, levobupivacaine, lidocaine, marcaine, mepivacaine, meprylcaine, metabutoxycaine, nitracaine, orthocaine, orabloc, oxetacaine, oxybuprocaine, paraethoxycaine, phenacaine, piperocaine, piridocaine, polocaine, posimir, pramocaine, prilocaine, primacaine, procaine, procainamide, proparacaine, propoxycaine, pyrrocaine, quinisocaine, ropivacaine, sensorcaine, septocaine, trimecaine, tetracaine, tolycaine, tropacocaine, ulcerease, xylocaine, zorcaine, decarbamoyl saxitoxin, gonyautoxins, or derivatives thereof. In some embodiments, the therapeutic agent is bupivacaine. In some embodiments, the therapeutic agent is a free base form of bupivacaine. In some embodiments, the therapeutic agent is an anti-cancer agent (e.g., anti-estrogens (e.g., tamoxifen, raloxifene, and megestrol), LHRH agonists (e.g., goscrclin and leuprolide), anti-androgens (e.g., flutamide and bicalutamide), photodynamic therapies (e.g., vertoporfin (BPD-MA), phthalocyanine, photosensitizer Pc4, and demethoxy-hypocrellin A (2BA-2- DMHA)), nitrogen mustards (e.g., cyclophosphamide, ifosfamide, trofosfamide, chlorambucil, estramustine, and melphalan), nitrosoureas (e.g., carmustine (BCNU) and lomustine (CCNU)), alkylsulphonates (e.g., busulfan and treosulfan), triazenes (e.g., dacarbazine, temozolomide), #13447332v2 platinum containing compounds (e.g., cisplatin, carboplatin, oxaliplatin), vinca alkaloids (e.g., vincristine, vinblastine, vindesine, and vinorelbine), taxoids (e.g., paclitaxel or a paclitaxel equivalent such as nanoparticle albumin-bound paclitaxel (Abraxane), docosahexaenoic acid bound-paclitaxel (DHA-paclitaxel, Taxoprexin), polyglutamate bound-paclitaxel (PG-paclitaxel, paclitaxel poliglumex, CT-2103, XYOTAX), the tumor-activated prodrug (TAP) ANG1005 (Angiopep-2 bound to three molecules of paclitaxel), paclitaxel-EC-1 (paclitaxel bound to the erbB2-recognizing peptide EC-1), and glucose-conjugated paclitaxel, e.g., ’2’-paclitaxel methyl 2-glucopyranosyl succinate; docetaxel, taxol), epipodophyllins (e.g., etoposide, etoposide phosphate, teniposide, topotecan, 9-aminocamptothecin, camptoirinotecan, irinotecan, crisnatol, mytomycin C), anti-metabolites, DHFR inhibitors (e.g., methotrexate, dichloromethotrexate, trimetrexate, edatrexate), IMP dehydrogenase inhibitors (e.g., mycophenolic acid, tiazofurin, ribavirin, and EICAR), ribonuclotide reductase inhibitors (e.g., hydroxyurea and deferoxamine), uracil analogs (e.g., 5-fluorouracil (5-FU), floxuridine, doxifluridine, ratitrexed, tegafur-uracil, capecitabine), cytosine analogs (e.g., cytarabine (ara C), cytosine arabinoside, and fludarabine), purine analogs (e.g., mercaptopurine and Thioguanine), Vitamin D3 analogs (e.g., EB 1089, CB 1093, and KH 1060), isoprenylation inhibitors (e.g., lovastatin), dopaminergic neurotoxins (e.g., 1-methyl-4-phenylpyridinium ion), cell cycle inhibitors (e.g., staurosporine), actinomycin (e.g., actinomycin D, dactinomycin), bleomycin (e.g., bleomycin A2, bleomycin B2, peplomycin), anthracycline (e.g., daunorubicin, doxorubicin, pegylated liposomal doxorubicin, idarubicin, epirubicin, pirarubicin, zorubicin, mitoxantrone), MDR inhibitors (e.g., verapamil), Ca2+ATPase inhibitors (e.g., thapsigargin), imatinib, thalidomide, lenalidomide, tyrosine kinase inhibitors (e.g., axitinib (AG013736), bosutinib (SKI-606), cediranib (RECENTINTM, AZD2171), dasatinib (SPRYCEL®, BMS-354825), erlotinib (TARCEVA®), gefitinib (IRESSA®), imatinib (Gleevec®, CGP57148B, STI-571), lapatinib (TYKERB®, TYVERB®), lestaurtinib (CEP-701), neratinib (HKI-272), nilotinib (TASIGNA®), semaxanib (semaxinib, SU5416), sunitinib (SUTENT®, SU11248), toceranib (PALLADIA®), vandetanib (ZACTIMA®, ZD6474), vatalanib (PTK787, PTK / ZK), trastuzumab (HERCEPTIN®), bevacizumab (AVASTIN®), rituximab (RITUXAN®), cetuximab (ERBITUX®), panitumumab (VECTIBIX®), ranibizumab (Lucentis®), nilotinib (TASIGNA®), sorafenib (NEXAVAR®), everolimus (AFINITOR®), alemtuzumab (CAMPATH®), gemtuzumab ozogamicin (MYLOTARG®), temsirolimus (TORISEL®), ENMD- 2076, PCI-32765, AC220, dovitinib lactate (TKI258, CHIR-258), BIBW 2992 (TOVOKTM), SGX523, PF-04217903, PF-02341066, PF-299804, BMS-777607, ABT-869, MP470, BIBF 1120 (VARGATEF®), AP24534, JNJ-26483327, MGCD265, DCC-2036, BMS-690154, CEP- 11981, tivozanib (AV-951), OSI-930, MM-121, XL-184, XL-647, and / or XL228), proteasome inhibitors (e.g., bortezomib (Velcade)), mTOR inhibitors (e.g., rapamycin, temsirolimus (CCI- #13447332v2 779), everolimus (RAD-001), ridaforolimus, AP23573 (Ariad), AZD8055 (AstraZeneca), BEZ235 (Novartis), BGT226 (Norvartis), XL765 (Sanofi Aventis), PF-4691502 (Pfizer), GDC0980 (Genetech), SF1126 (Semafoe) and OSI-027 (OSI)), oblimersen, gemcitabine, carminomycin, leucovorin, pemetrexed, cyclophosphamide, dacarbazine, procarbizine, prednisolone, dexamethasone, campathecin, plicamycin, asparaginase, aminopterin, methopterin, porfiromycin, melphalan, leurosidine, leurosine, chlorambucil, trabectedin, procarbazine, discodermolide, carminomycin,, aminopterin, or hexamethyl melamine). In some embodiments, the therapeutic agent is a taxoid (e.g., paclitaxel or a paclitaxel equivalent such as nanoparticle albumin-bound paclitaxel (Abraxane), docosahexaenoic acid bound-paclitaxel (DHA-paclitaxel, Taxoprexin), polyglutamate bound-paclitaxel (PG-paclitaxel, paclitaxel poliglumex, CT-2103, XYOTAX), the tumor-activated prodrug (TAP) ANG1005 (Angiopep-2 bound to three molecules of paclitaxel), paclitaxel-EC-1 (paclitaxel bound to the erbB2- recognizing peptide EC-1), or glucose-conjugated paclitaxel, e.g., ’2’-paclitaxel methyl 2- glucopyranosyl succinate; docetaxel, taxol). In some embodiments, the therapeutic agent is a free base form of an anti-cancer agent. In some embodiments, the anti-cancer agent is not doxorubicin. In some embodiments, the therapeutic agent is paclitaxel. In some embodiments, the therapeutic agent is a free base form of paclitaxel. In some embodiments, the therapeutic agent is an antihistamine (e.g., diphenhydramine, chlorpheniramine, cetirizine, loratadine, fexofenadine, levocetirizine, desloratadine, Brompheniramine, Clemastine, Cyproheptadine, Dexchlorpheniramine Dimenhydrinate, Doxylamine Hydroxyzine, Phenindamine, Azelastine, Cimetidine, Famotidine, Nizatidine, or Ranitidine). In some embodiments, the therapeutic agent is diphenhydramine, chlorpheniramine, cetirizine, loratadine, fexofenadine, levocetirizine, desloratadine, Brompheniramine, Clemastine, Cyproheptadine, Dexchlorpheniramine Dimenhydrinate, Doxylamine Hydroxyzine, Phenindamine, Azelastine, Cimetidine, Famotidine, Nizatidine, or Ranitidine. In some embodiments, the therapeutic agent is a free base form of an antihistamine. In some embodiments, the therapeutic agent is diphenhydramine. In some embodiments, the therapeutic agent is a free base form of diphenhydramine. In some embodiments, the composition comprises an effective amount of the therapeutic agent. In some embodiments, the composition comprises a therapeutically effective amount of the therapeutic agent. In some embodiments, the composition comprises a prophylactically effective amount of the therapeutic agent. In some embodiments, the effective amount is an amount effective for treating a disease or disorder that would benefit from administration of a therapeutic agent in a subject in need thereof. In some embodiments, the effective amount is an #13447332v2 amount effective for preventing a disease or disorder that would benefit from administration of a therapeutic agent in a subject in need thereof. In some embodiments, the effective amount is an amount effective for reducing the risk of developing a disease or disorder that would benefit from administration of a therapeutic agent in a subject in need thereof. In some embodiments, the amount of the therapeutic agent in the composition is about 1%, about 2%, about 3%, about 4%, about 5%, about 6%, about 7%, about 8%, about 9%, about 10%, about 11%, about 12%, about 13%, about 14%, about 15%, about 16%, about 17%, about 18%, about 19%, about 20%, about 21%, about 22%, about 23%, about 24%, about 25%, about 26%, about 27%, about 28%, about 29%, about 30%, about 40%, about 40%, about 50%, about 60%, about 70%, about 80%, about 90%, or about 100% greater than the amount of the therapeutic agent in a composition that is not a composition disclosed herein. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of between about 5 mg / mL and about 100 mg / mL, between about 5 mg / mL and about 90 mg / mL, between about 5 mg / mL and about 80 mg / mL, between about 5 mg / mL and about 70 mg / mL, between about 5 mg / mL and about 60 mg / mL, between about 5 mg / mL and about 50 mg / mL, between about 5 mg / mL and about 40 mg / mL, between about 5 mg / mL and about 30 mg / mL, between about 5 mg / mL and about 25 mg / mL, between about 5 mg / mL and about 22.5 mg / mL, between about 5 mg / mL and about 20 mg / mL, between about 10 mg / mL and about 100 mg / mL, between about 10 mg / mL and about 90 mg / mL, between about 10 mg / mL and about 80 mg / mL, between about 10 mg / mL and about 70 mg / mL, between about 10 mg / mL and about 60 mg / mL, between about 10 mg / mL and about 50 mg / mL, between about 10 mg / mL and about 40 mg / mL, between about 10 mg / mL and about 30 mg / mL, between about 10 mg / mL and about 25 mg / mL, between about 10 mg / mL and about 22.5 mg / mL, between about 10 mg / mL and about 20 mg / mL, between about 15 mg / mL and about 100 mg / mL, between about 15 mg / mL and about 90 mg / mL, between about 15 mg / mL and about 80 mg / mL, between about 15 mg / mL and about 70 mg / mL, between about 15 mg / mL and about 60 mg / mL, between about 15 mg / mL and about 50 mg / mL, between about 15 mg / mL and about 40 mg / mL, between about 15 mg / mL and about 30 mg / mL, between about 15 mg / mL and about 25 mg / mL, between about 15 mg / mL and about 22.5 mg / mL, between about 15 mg / mL and about 20 mg / mL, between about 17.5 mg / mL and about 100 mg / mL, between about 17.5 mg / mL and about 90 mg / mL, between about 17.5 mg / mL and about 80 mg / mL, between about 17.5 mg / mL and about 70 mg / mL, between about 17.5 mg / mL and about 60 mg / mL, between about 17.5 mg / mL and about 50 mg / mL, between about 17.5 mg / mL and about 40 mg / mL, between about 17.5 mg / mL and about 30 mg / mL, between about 17.5 mg / mL and about 25 mg / mL, between about 17.5 mg / mL and about 22.5 mg / mL, between about 17.5 mg / mL and about 20 mg / mL, between about 20 #13447332v2 mg / mL and about 100 mg / mL, between about 20 mg / mL and about 90 mg / mL, between about 20 mg / mL and about 80 mg / mL, between about 20 mg / mL and about 70 mg / mL, between about 20 mg / mL and about 60 mg / mL, between about 20 mg / mL and about 50 mg / mL, between about 20 mg / mL and about 40 mg / mL, between about 20 mg / mL and about 30 mg / mL, between about 20 mg / mL and about 25 mg / mL, or between about 20 mg / mL and about 22.5 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of between about 5 mg / mL and about 100 mg / mL, between about 5 mg / mL and about 50 mg / mL, between about 10 mg / mL and about 40 mg / mL, between about 10 mg / mL and about 30 mg / mL, between about 15 mg / mL and about 30 mg / mL, between about 15 mg / mL and about 25 mg / mL, between about 17.5 mg / mL and about 25 mg / mL, or between about 17.5 mg / mL and about 22.5 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of between about 5 mg / mL and about 100 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of between about 5 mg / mL and about 50 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of between about 10 mg / mL and about 40 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of between about 10 mg / mL and about 30 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of between about 15 mg / mL and about 30 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of between about 15 mg / mL and about 25 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of between about 17.5 mg / mL and about 25 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of between about 17.5 mg / mL and about 22.5 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 5 mg / mL, about 10 mg / mL, about 15 mg / mL, about 17.5 mg / mL, about 20 mg / mL, about 22.5 mg / mL, about 25 mg / mL, about 30 mg / mL, about 35 mg / mL, about 40 mg / mL, about 45 mg / mL, about 50 mg / mL, about 60 mg / mL, about 70 mg / mL, about 80 mg / mL, about 90 mg / mL, or about 100 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 5 mg / mL, about 10 mg / mL, about 15 mg / mL, about 17.5 mg / mL, about 20 mg / mL, about 22.5 mg / mL, about 25 mg / mL, about 30 mg / mL, about 35 mg / mL, or about 40 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 5 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 10 mg / mL. In some #13447332v2 embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 15 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 17.5 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 20 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 22.5 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 25 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 30 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 35 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 40 mg / mL. Embodiments of the Composition In some embodiments, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the crosslinking agent is glutaraldehyde, and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is an anesthetic, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is an anesthetic, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is an anesthetic, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is an anesthetic, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is an anesthetic, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is an anesthetic, the crosslinking agent is glutaraldehyde, and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an anesthetic, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an anesthetic, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some #13447332v2 embodiments, the therapeutic agent is a free base form of an anesthetic, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an anesthetic, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an anesthetic, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is a free base form of an anesthetic, the crosslinking agent is glutaraldehyde, and the protein is alpha-1- acid glycoprotein. In some embodiments, the therapeutic agent is bupivacaine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is bupivacaine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is bupivacaine, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is bupivacaine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is bupivacaine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is bupivacaine, the crosslinking agent is glutaraldehyde, and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of bupivacaine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of bupivacaine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is a free base form of bupivacaine, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of bupivacaine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of bupivacaine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is a free base form of bupivacaine, the crosslinking agent is glutaraldehyde, and the protein is alpha-1- acid glycoprotein. In some embodiments, the composition is characterized in that, when tested in vitro by placing the composition in a medium, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 168 hours after placing the #13447332v2 composition in the medium. In some embodiments, the composition is characterized in that, when tested in vitro by placing the composition in a medium, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 144 hours after placing the composition in the medium. In some embodiments, the composition is characterized in that, when tested in vitro by placing the composition in a medium, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 120 hours after placing the composition in the medium. In some embodiments, the composition is characterized in that, when tested in vitro by placing the composition in a medium, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 96 hours after placing the composition in the medium. In some embodiments, the composition is characterized in that, when tested in vitro by placing the composition in a medium, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 72 hours after placing the composition in the medium. In some embodiments, the composition is characterized in that, when tested in vitro by placing the composition in a medium, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 48 hours after placing the composition in the medium. In some embodiments, the composition is characterized in that, when tested in vitro by placing the composition in a medium, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 24 hours after placing the composition in the medium. In some embodiments, the composition is characterized in that, when tested in vitro by placing the composition in a medium, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 12 hours after placing the composition in the medium. In some embodiments, the composition is characterized in that, when tested in vitro by placing the composition in a medium, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 6 hours after placing the composition in the medium. In some embodiments, the composition is characterized in that, when tested in vitro by placing the #13447332v2 composition in a medium, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 3 hours after placing the composition in the medium. In some embodiments, the medium is physiological saline or phosphate-buffered saline (PBS) having a pH of about 7.4. In some embodiments, the composition is characterized in that, when administered to a subject, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 168 hours after administration of the composition. In some embodiments, the composition is characterized in that, when administered to a subject, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 144 hours after administration of the composition. In some embodiments, the composition is characterized in that, when administered to a subject, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 120 hours after administration of the composition. In some embodiments, the composition is characterized in that, when administered to a subject, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 96 hours after administration of the composition. In some embodiments, the composition is characterized in that, when administered to a subject, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 72 hours after administration of the composition. In some embodiments, the composition is characterized in that, when administered to a subject, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 48 hours after administration of the composition. In some embodiments, the composition is characterized in that, when administered to a subject, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 24 hours after administration of the composition. In some embodiments, the composition is characterized in that, when administered to a subject, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from #13447332v2 the composition 12 hours after administration of the composition. In some embodiments, the composition is characterized in that, when administered to a subject, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 6 hours after administration of the composition. In some embodiments, the composition is characterized in that, when administered to a subject, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 3 hours after administration of the composition. In some embodiments, the composition is characterized in that, when administered to a subject, duration of a therapeutic effect is extended by at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, or at least 200% compared to duration of the therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a composition of the present disclosure. In some embodiments, the therapeutic effect is nerve block and / or reduced pain. In some embodiments, the therapeutic effect is nerve block. In some embodiments, the therapeutic effect is sciatic nerve block. In some embodiments, the therapeutic effect is reduced pain. In some embodiments, the therapeutic effect is treatment of a cancer (e.g., reduction of the size of a tumor). In some embodiments, the therapeutic effect is reduction of the size of a tumor. In some embodiments, the therapeutic effect is treatment of an allergy. In some embodiments, the composition exhibits a honeycomb-like structure with pores having a diameter of between about 1 μm and about 25 μm in size, between about 1 μm and about 20 μm in size, between about 1 μm and about 15 μm in size, between about 1 μm and about 14 μm in size, between about 1 μm and about 13 μm in size, between about 1 μm and about 12.5 μm in size, between about 1 μm and about 12 μm in size, between about 1 μm and about 11 μm in size, between about 1 μm and about 10 μm in size, between about 2.5 μm and about 25 μm in size, between about 2.5 μm and about 20 μm in size, between about 2.5 μm and about 15 μm in size, between about 2.5 μm and about 14 μm in size, between about 2.5 μm and about 13 μm in size, between about 2.5 μm and about 12.5 μm in size, between about 2.5 μm and about 12 μm in size, between about 2.5 μm and about 11 μm in size, between about 2.5 μm and about 10 μm in size, between about 5 μm and about 25 μm in size, between about 5 μm and about 20 μm in size, between about 5 μm and about 15 μm in size, between about 5 μm and about 14 μm in size, between about 5 μm and about 13 μm in size, between about 5 μm and about 12.5 μm in size, between about 5 μm and about 12 μm in size, between about 5 μm and about 11 μm in size, or between about 5 μm and about 10 μm in size. In some embodiments, the #13447332v2 composition exhibits a honeycomb-like structure with pores having a diameter of between about 1 μm and about 25 μm in size. In some embodiments, the composition exhibits a honeycomb- like structure with pores having a diameter of between about 1 μm and about 15 μm in size. In some embodiments, the composition exhibits a honeycomb-like structure with pores having a diameter of between about 2.5 μm and about 12.5 μm in size. In some embodiments, the composition exhibits a honeycomb-like structure with pores having a diameter of between about 5 μm and about 10 μm in size. In some embodiments, the honeycomb-like structure comprises hexagonal pores. In some embodiments, the honeycomb-like structure comprises a hexagonal cavity. In some embodiments, the composition comprises a storage modulus (G′) that is greater than a loss modulus (G′′) at a temperature of about 0 ℃, about 5 ℃, about 10 ℃, about 15 ℃, about 16 ℃, about 17 ℃, about 18 ℃, about 19 ℃, about 20 ℃, about 21 ℃, about 22 ℃, about 23 ℃, about 24 ℃, about 25 ℃, about 26 ℃, about 27 ℃, about 28 ℃, about 29 ℃, about 30 ℃, about 31 ℃, about 32 ℃, about 33 ℃, about 34 ℃, about 35 ℃, about 36 ℃, about 37 ℃, about 38 ℃, about 39 ℃, about 40 ℃, about 45 ℃, or about 50 ℃. In some embodiments, the composition comprises a storage modulus (G′) that is greater than a loss modulus (G′′) at a temperature of about 25 ℃. In some embodiments, the composition is injectable. In some embodiments, the composition is biodegradable. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of between about 10 mg / mL and about 50 mg / mL, the bovine serum albumin is present in a concentration of between about 25 mg / mL and about 125 mg / mL, and the glutaraldehyde is present in a concentration of between about 1 mg / mL and about 15 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of between about 10 mg / mL and about 50 mg / mL, the bovine serum albumin is present in a concentration of between about 37.5 mg / mL and about 112.5 mg / mL, and the glutaraldehyde is present in a concentration of between about 2.5 mg / mL and about 12.5 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of between about 10 mg / mL and about 50 mg / mL, the bovine serum albumin is present in a concentration of between about 45 mg / mL and about 105 mg / mL, and the glutaraldehyde is present in a concentration of between about 4.5 mg / mL and about 10.5 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of between about 10 mg / mL and about 50 mg / mL, the bovine serum albumin is present in a concentration of between about 50 mg / mL and about 100 mg / mL, and the glutaraldehyde is present in a concentration of between about 5 mg / mL and about 10 mg / mL. #13447332v2 In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 20 mg / mL, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 20 mg / mL, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 20 mg / mL, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the therapeutic agent is bupivacaine present in the composition in a concentration of about 20 mg / mL, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the therapeutic agent is an anti-cancer agent, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is an anti-cancer agent, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is an anti-cancer agent, the crosslinking agent is of Formula (II), and the protein is alpha- 1-acid glycoprotein. In some embodiments, the therapeutic agent is an anti-cancer agent, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is an anti-cancer agent, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is an anti-cancer agent, the crosslinking agent is glutaraldehyde, and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an anti-cancer agent, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1- acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an anti- cancer agent, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is a free base form of an anti-cancer agent, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an anti-cancer agent, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an anti-cancer agent, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is a free base form of an anti-cancer agent, the crosslinking agent is glutaraldehyde, and the protein is alpha-1-acid glycoprotein. #13447332v2 In some embodiments, the therapeutic agent is paclitaxel, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is paclitaxel, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is paclitaxel, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is paclitaxel, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is paclitaxel, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is paclitaxel, the crosslinking agent is glutaraldehyde, and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is paclitaxel present in the composition in a concentration of between about 0.1 mg / mL and about 10 mg / mL, the bovine serum albumin is present in a concentration of between about 25 mg / mL and about 125 mg / mL, and the glutaraldehyde is present in a concentration of between about 1 mg / mL and about 15 mg / mL. In some embodiments, the therapeutic agent is paclitaxel present in the composition in a concentration of between about 0.1 mg / mL and about 10 mg / mL, the bovine serum albumin is present in a concentration of between about 37.5 mg / mL and about 112.5 mg / mL, and the glutaraldehyde is present in a concentration of between about 2.5 mg / mL and about 12.5 mg / mL. In some embodiments, the therapeutic agent is paclitaxel present in the composition in a concentration of between about 0.1 mg / mL and about 10 mg / mL, the bovine serum albumin is present in a concentration of between about 45 mg / mL and about 105 mg / mL, and the glutaraldehyde is present in a concentration of between about 4.5 mg / mL and about 10.5 mg / mL. In some embodiments, the therapeutic agent is paclitaxel present in the composition in a concentration of between about 0.1 mg / mL and about 10 mg / mL, the bovine serum albumin is present in a concentration of between about 50 mg / mL and about 100 mg / mL, and the glutaraldehyde is present in a concentration of between about 5 mg / mL and about 10 mg / mL. In some embodiments, the therapeutic agent is paclitaxel present in the composition in a concentration of about 1 mg / mL, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the therapeutic agent is paclitaxel present in the composition in a concentration of about 1 mg / mL, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the therapeutic agent is paclitaxel present in the composition in a concentration of about 1 mg / mL, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In #13447332v2 some embodiments, the therapeutic agent is paclitaxel present in the composition in a concentration of about 1 mg / mL, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the therapeutic agent is an antihistamine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is an antihistamine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is an antihistamine, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is an antihistamine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is an antihistamine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is an antihistamine, the crosslinking agent is glutaraldehyde, and the protein is alpha-1- acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an antihistamine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an antihistamine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is a free base form of an antihistamine, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an antihistamine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an antihistamine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is a free base form of an antihistamine, the crosslinking agent is glutaraldehyde, and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is diphenydramine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is diphenydramine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is diphenydramine, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is diphenydramine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is diphenydramine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic #13447332v2 agent is diphenydramine, the crosslinking agent is glutaraldehyde, and the protein is alpha-1- acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of diphenydramine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of diphenydramine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is a free base form of diphenydramine, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of diphenydramine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of diphenydramine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is a free base form of diphenydramine, the crosslinking agent is glutaraldehyde, and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is diphenydramine present in the composition in a concentration of between about 0.1 mg / mL and about 10 mg / mL, the bovine serum albumin is present in a concentration of between about 25 mg / mL and about 125 mg / mL, and the glutaraldehyde is present in a concentration of between about 1 mg / mL and about 15 mg / mL. In some embodiments, the therapeutic agent is diphenydramine present in the composition in a concentration of between about 0.1 mg / mL and about 10 mg / mL, the bovine serum albumin is present in a concentration of between about 37.5 mg / mL and about 112.5 mg / mL, and the glutaraldehyde is present in a concentration of between about 2.5 mg / mL and about 12.5 mg / mL. In some embodiments, the therapeutic agent is diphenydramine present in the composition in a concentration of between about 0.1 mg / mL and about 10 mg / mL, the bovine serum albumin is present in a concentration of between about 45 mg / mL and about 105 mg / mL, and the glutaraldehyde is present in a concentration of between about 4.5 mg / mL and about 10.5 mg / mL. In some embodiments, the therapeutic agent is diphenydramine present in the composition in a concentration of between about 0.1 mg / mL and about 10 mg / mL, the bovine serum albumin is present in a concentration of between about 50 mg / mL and about 100 mg / mL, and the glutaraldehyde is present in a concentration of between about 5 mg / mL and about 10 mg / mL. In some embodiments, the therapeutic agent is diphenydramine present in the composition in a concentration of about 1 mg / mL, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the therapeutic agent is diphenydramine present in the #13447332v2 composition in a concentration of about 1 mg / mL, the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. In some embodiments, the therapeutic agent is diphenydramine present in the composition in a concentration of about 1 mg / mL, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL. In some embodiments, the therapeutic agent is diphenydramine present in the composition in a concentration of about 1 mg / mL, the bovine serum albumin is present in a concentration of about 100 mg / mL, and the glutaraldehyde is present in a concentration of about 10 mg / mL. Pharmaceutical Compositions, Kits, and Administration The present disclosure provides compositions comprising a hydrogel and a protein- stabilized nanoparticle, wherein: the hydrogel comprises a crosslinked protein matrix; the protein-stabilized nanoparticle comprises a therapeutic agent or a diagnostic agent; and the protein-stabilized nanoparticle is embedded in the crosslinked protein matrix. In some embodiments, the composition is a pharmaceutical composition. In some embodiments, the composition further comprises a pharmaceutically acceptable excipient. In some embodiments, the pharmaceutical composition comprises an effective amount of a therapeutic agent. In some embodiments, the effective amount is a therapeutically effective amount. In some embodiments, the effective amount is a prophylactically effective amount. In some embodiments, the effective amount is an amount effective for treating a disease or condition in a subject in need thereof. In some embodiments, the effective amount is an amount effective for preventing a disease or condition in a subject in need thereof. In some embodiments, the effective amount is an amount effective for reducing the risk of developing a disease or condition in a subject in need thereof. Compositions described herein can be prepared by any method known in the art of pharmacology. In general, such preparatory methods comprise the steps disclosed herein. In some embodiments, the preparation further comprises adding and / or one or more other accessory ingredients, and then, if necessary and / or desirable, shaping and / or packaging the product into a desired single- or multi-dose unit. Pharmaceutical compositions can be prepared, packaged, and / or sold in bulk, as a single unit dose, and / or as a plurality of single unit doses. As used herein, a “unit dose” is a discrete amount of the pharmaceutical composition comprising a predetermined amount of the active #13447332v2 ingredient. The amount of the active ingredient is generally equal to the dosage of the active ingredient which would be administered to a subject and / or a convenient fraction of such a dosage, such as, for example, one-half or one-third of such a dosage. The compositions provided herein can be administered by any route, including enteral (e.g., oral), parenteral, intravenous, intramuscular, intra-arterial, intramedullary, intrathecal, subcutaneous, intraventricular, transdermal, interdermal, rectal, intravaginal, intraperitoneal, topical, mucosal, nasal, bucal, sublingual; by intratracheal instillation, bronchial instillation, and / or inhalation; and / or as an oral spray, nasal spray, and / or aerosol. A composition, as described herein, can be administered in combination with one or more additional agents (e.g., pharmaceutical agent, e.g., therapeutically and / or prophylactically active agents). The compositions can be administered in combination with additional pharmaceutical agents that improve their activity (e.g., activity (e.g., potency and / or efficacy) in treating a disease in a subject in need thereof, in preventing a disease in a subject in need thereof, and / or in reducing the risk to develop a disease in a subject in need thereof), improve bioavailability, improve their ability to cross the blood-brain barrier, improve safety, reduce drug resistance, reduce and / or modify metabolism, inhibit excretion, and / or modify distribution in a subject or cell. It will also be appreciated that the therapy employed may achieve a desired effect for the same disorder, and / or it may achieve different effects. In some embodiments, a pharmaceutical composition described herein including a therapeutic agent described herein and an additional agent exhibits a synergistic effect that is absent in a pharmaceutical composition including one of the therapeutic agent and the additional agent, but not both. In some embodiments, the additional agent is a therapeutic agent. The composition can be administered concurrently with, prior to, or subsequent to one or more additional pharmaceutical agents, which may be useful as, e.g., combination therapies. Pharmaceutical agents include therapeutically active agents. Pharmaceutical agents also include prophylactically active agents. Pharmaceutical agents include small organic molecules such as drug compounds (e.g., compounds approved for human or veterinary use by the U.S. Food and Drug Administration as provided in the Code of Federal Regulations (CFR)), peptides, proteins, carbohydrates, monosaccharides, oligosaccharides, polysaccharides, nucleoproteins, mucoproteins, lipoproteins, synthetic polypeptides or proteins, small molecules linked to proteins, glycoproteins, steroids, nucleic acids, DNAs, RNAs, nucleotides, nucleosides, oligonucleotides, antisense oligonucleotides, lipids, hormones, vitamins, and cells. Each additional pharmaceutical agent may be administered at a dose and / or on a time schedule determined for that pharmaceutical agent. The additional pharmaceutical agents may also be administered together with each other and / or with the compound or composition described #13447332v2 herein in a single dose or administered separately in different doses. The particular combination to employ in a regimen will take into account compatibility of the compound described herein with the additional pharmaceutical agent(s) and / or the desired therapeutic and / or prophylactic effect to be achieved. In general, it is expected that the additional pharmaceutical agent(s) in combination be utilized at levels that do not exceed the levels at which they are utilized individually. In some embodiments, the levels utilized in combination will be lower than those utilized individually. In some embodiments, the subject is an animal. The animal may be of either sex and may be at any stage of development. In some embodiments, the subject described herein is a human. In some embodiments, the subject is a non-human animal. In some embodiments, the subject is a mammal. In some embodiments, the subject is a non-human mammal. In some embodiments, the subject is a domesticated animal, such as a dog, cat, cow, pig, horse, sheep, or goat. In some embodiments, the subject is a companion animal, such as a dog or cat. In some embodiments, the subject is a livestock animal, such as a cow, pig, horse, sheep, or goat. In some embodiments, the subject is a zoo animal. In another embodiment, the subject is a research animal, such as a rodent (e.g., mouse, rat), dog, pig, or non-human primate. In some embodiments, the animal is a genetically engineered animal. In some embodiments, the animal is a transgenic animal (e.g., transgenic mice and transgenic pigs). In some embodiments, the subject is a fish or reptile. Also encompassed by the disclosure are kits (e.g., pharmaceutical packs). The kits provided comprise a composition described herein and instructions for using the kit. The kits provided may comprise a composition described herein and a container (e.g., a vial, ampule, bottle, syringe, and / or dispenser package, or other suitable container). In some embodiments, provided kits may optionally further include a second container comprising a pharmaceutical excipient for dilution or suspension of a composition described herein. In some embodiments, the composition described herein provided in the first container and the second container are combined to form one unit dosage form. Thus, in one aspect, provided are kits including a first container comprising a composition described herein. In some embodiments, the kits are useful for treating a disease or condition (e.g., pain) in a subject in need thereof. In some embodiments, the kits are useful for preventing a disease or condition (e.g., pain) in a subject in need thereof. In some embodiments, the kits are useful for reducing the risk of developing a disease or condition (e.g., pain) in a subject in need thereof. A kit described herein may also include information as required by a regulatory agency such as the U.S. Food and Drug Administration (FDA). In some embodiments, the information #13447332v2 included in the kits is prescribing information. In some embodiments, a kit described herein may include one or more additional pharmaceutical agents described herein as a separate composition. Methods of Use The present disclosure also provides methods for treating diseases or conditions in a subject in need thereof, the methods comprising administering to the subject a provided composition. The present disclosure also provides methods for preventing diseases or conditions in a subject in need thereof, the methods comprising administering to the subject a provided composition. The present disclosure also provides methods for reducing the risk of developing a disease or condition in a subject in need thereof. In some embodiments, the disclosed compositions can be used to treat a subject (e.g., a human) having a disease or condition that would benefit from administration of a therapeutic agent. In some embodiments, the subject is administered an effective amount of any one or more disclosed compositions. In some embodiments, the subject is administered a therapeutically effective amount of any one or more disclosed compositions. In some embodiments, the subject is administered a prophylactically effective amount of any one or more disclosed compositions. In some embodiments, the subject is an animal. In some embodiments, the subject is a mammal. In some embodiments, the subject is a human. In some embodiments, the subject is a human aged 18 years or older. In some embodiments, the subject is a human aged 12-18 years, exclusive. In some embodiments, the subject is a human aged 2-12 years, inclusive. In some embodiments, the subject is a human younger than 2 years. In some embodiments, the subject is a non-human animal. In some embodiments, the subject is a non-human mammal. In some embodiments, the disease or condition being treated is one associated with a specific biological target. In some embodiments, the target is a voltage-gated sodium channel. In some embodiments, the target is a site-1 sodium channel. In some embodiments, the disease or condition is pain. The quality of life of patients suffering from postoperative or even chronic pain is often diminished by the need for repeated administration of systemic analgesic medications (e.g., opioids), which give rise to potentially serious complications and clouding of the sensorium. Typically, repeated administration of systemic analgesic medications requires that patients be tethered to an external device, which can prolong hospitalization and even require that recipients be maintained as inpatients. Further, existing pain management options limit the ability of patients suffering from postoperative pain or chronic pain to adjust the timing, intensity and duration of anesthetic effect. #13447332v2 Peripheral nerves are surrounded by the perineurium, which is composed of a basal membrane with a layer of perineurial cells and tight junctions limiting paracellular permeability. Delivery of analgesic drugs is often impeded by the perineurium. For example, tetrodotoxin (TTX) is an attractive candidate in peripheral nerve anesthesia because of its reduced affinity for voltage dependent sodium channels of the peripheral nerve, but a poor affinity for the cardiac sodium channel isoform. It also does not cross the blood brain barrier. Voltage-gated sodium channels play important roles in nociceptive nerve conduction, but candidate anesthetics (e.g., specific antagonists of sodium channels) are often not effective in vivo because of lack of permeability of the perineurial barrier. Hence, high concentrations of anesthetics and multiple dosages are often required to achieve clinically effective and prolonged anesthesia. Although permeation enhancers have been used to increase the permeability of lipid barriers and, they can be associated with myotoxicity. There exists a need for systems for the delivery of local anesthetic that can provide repeated or prolonged analgesia on-demand, following a single administration. In some embodiments, the methods for treating diseases or conditions comprise administering the composition such that the therapeutic agent is delivered to a biological target at a rate that is less than if the therapeutic agent were administered alone. In such embodiments, the therapeutic agent is delivered via sustained release. In some embodiments, the administration is local such that the sustained release is a local sustained release (i.e., local administration for a local effect, e.g., subcutaneous administration). In some embodiments, administration is systemic such that the sustained release is a systemic sustained release (i.e., systemic administration for a dispersed or system-wide effect, e.g., parenteral administration). In some embodiments, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 168 hours after administration of the composition to the subject. In some embodiments, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 144 hours after administration of the composition to the subject. In some embodiments, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 120 hours after administration of the composition to the subject. In some embodiments, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 96 hours after administration of the composition to the subject. In some #13447332v2 embodiments, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 72 hours after administration of the composition to the subject. In some embodiments, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 48 hours after administration of the composition to the subject. In some embodiments, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 24 hours after administration of the composition to the subject. In some embodiments, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 12 hours after administration of the composition to the subject. In some embodiments, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 6 hours after administration of the composition to the subject. In some embodiments, less than 100%, less than 90%, less than 80%, less than 70%, less than 60%, less than 50%, less than 40%, less than 30%, less than 20%, or less than 10% of the therapeutic agent is released from the composition 3 hours after administration of the composition to the subject. In some embodiments, duration of a therapeutic effect is extended by at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, at least 200%, at least 300%, at least 400%, at least 500%, at least 600%, at least 700%, at least 800%, at least 900%, at least 1,000%, or at least 10,000% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by at least 10% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by at least 20% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by at least 30% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by at least 40% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a #13447332v2 therapeutic effect is extended by at least 50% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by at least 60% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by at least 70% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by at least 80% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by at least 90% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by at least 100% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by least 200% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by least 300% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by least 400% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by least 500% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by least 600% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by least 700% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by least 800% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by least 900% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a #13447332v2 therapeutic effect is extended by least 1,000% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, duration of a therapeutic effect is extended by least 10,000% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not a provided composition. In some embodiments, the therapeutic effect is nerve block and / or reduced pain. In some embodiments, the therapeutic effect is nerve block or reduced pain. In some embodiments, the therapeutic effect is nerve block and reduced pain. In some embodiments, the therapeutic effect is nerve block. In some embodiments, the therapeutic effect is sciatic nerve block. In some embodiments, the therapeutic effect is reduced pain. In some embodiments, the therapeutic effect is reduction of pain by at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, or at least 99% compared to a baseline level of pain prior to administration. The present disclosure also provides uses of a provided composition in a method described herein. The present disclosure also provides uses of a provided pharmaceutical composition in a method described herein. The present disclosure also provides a provided composition for use in a method described herein. The present disclosure also provides a provided pharmaceutical composition for use in a method described herein. Methods of Preparation The present disclosure also provides methods for preparing a provided composition, wherein the method comprises: providing a therapeutic agent or a diagnostic agent; forming a protein-stabilized nanoparticle comprising the therapeutic agent or the diagnostic agent by exposing the therapeutic agent or the diagnostic agent to a solution of a protein in water; and reacting the protein with a crosslinking agent, thereby producing a crosslinked protein matrix. In some embodiments, providing the therapeutic agent or the diagnostic agent further comprises forming a free base form of the therapeutic agent or the diagnostic agent. In some embodiments, the free base form of the therapeutic agent or the diagnostic agent is formed by reacting a salt form of the therapeutic agent or the diagnostic agent with a base. In some embodiments, the method comprises providing a diagnostic agent. In some embodiments, providing the diagnostic agent further comprises forming a free base form of the #13447332v2 diagnostic agent. In some embodiments, the free base form of the diagnostic agent is formed by reacting a salt form of the diagnostic agent with a base. In some embodiments, the method comprises providing a therapeutic agent. In some embodiments, providing the therapeutic agent further comprises forming a free base form of the therapeutic agent. In some embodiments, the free base form of the therapeutic agent is formed by reacting a salt form of the therapeutic agent with a base. In some embodiments, the therapeutic agent is a small molecule or a biologic. In some embodiments, the therapeutic agent is a small molecule, a protein, or a nucleic acid. In some embodiments, the therapeutic agent is a small molecule. In some embodiments, the therapeutic agent is an anesthetic. In some embodiments, the therapeutic agent is a free base form of an anesthetic. In some embodiments, the therapeutic agent is hydrophobic. In some embodiments, the therapeutic agent is hydrohilic. In some embodiments, the therapeutic agent does not comprise a primary or secondary amine. In some embodiments, the therapeutic agent is not doxorubicin. In some embodiments, the therapeutic agent is a local anesthetic (e.g., tetrodotoxin, saxitoxin, neosaxitoxin, bupivacaine, amylocaine, ambucaine, articaine, benzocaine, benzonatate, butacaine, butanilicaine, carbocaine, cepastat, chloraseptic, chloroprocaine, cinchocaine, citanest, cyclomethycaine, dibucaine, diperodon, dimethocaine, eucaine, etidocaine, fomocaine, fotocaine, hydroxyprocaine, isobucaine, levobupivacaine, lidocaine, marcaine, mepivacaine, meprylcaine, metabutoxycaine, nitracaine, orthocaine, orabloc, oxetacaine, oxybuprocaine, paraethoxycaine, phenacaine, piperocaine, piridocaine, polocaine, posimir, pramocaine, prilocaine, primacaine, procaine, procainamide, proparacaine, propoxycaine, pyrrocaine, quinisocaine, ropivacaine, sensorcaine, septocaine, trimecaine, tetracaine, tolycaine, tropacocaine, ulcerease, xylocaine, or zorcaine). In some embodiments, the therapeutic agent is a free base form of a local anesthetic. In some embodiments, the therapeutic agent is a local anesthetic compound, for example, but not limited to, an amino ester compound (e.g., procaine, tetracaine, chloroprocaine, benzocaine, butacaine, dimethocaine) or an amino amide compound (e.g., procainamide, lidocaine). In some embodiments, the local anesthetic is a sodium channel blocker, for example, a site 1 sodium channel blocker (e.g., tetrodotoxin, saxitoxins (saxitoxin, neosaxitoxin), gonyautoxins (gonyautoxin V, gonyautoxin VI), µ- conotoxins)) or an amino amide local anesthetic. In some embodiments, the therapeutic agent is a site 1 sodium channel blocker, amino ester anesthetic, or an amino amide anesthetic, or a derivative thereof. In some embodiments, the therapeutic agent is tetrodotoxin, saxitoxin, neosaxitoxin, bupivacaine, amylocaine, ambucaine, articaine, benzocaine, benzonatate, butacaine, #13447332v2 butanilicaine, carbocaine, cepastat, chloraseptic, chloroprocaine, cinchocaine, citanest, cyclomethycaine, dibucaine, diperodon, dimethocaine, eucaine, etidocaine, fomocaine, fotocaine, hydroxyprocaine, isobucaine, levobupivacaine, lidocaine, marcaine, mepivacaine, meprylcaine, metabutoxycaine, nitracaine, orthocaine, orabloc, oxetacaine, oxybuprocaine, paraethoxycaine, phenacaine, piperocaine, piridocaine, polocaine, posimir, pramocaine, prilocaine, primacaine, procaine, procainamide, proparacaine, propoxycaine, pyrrocaine, quinisocaine, ropivacaine, sensorcaine, septocaine, trimecaine, tetracaine, tolycaine, tropacocaine, ulcerease, xylocaine, zorcaine, decarbamoyl saxitoxin, gonyautoxins, or derivatives thereof. In some embodiments, the therapeutic agent is bupivacaine. In some embodiments, the therapeutic agent is a free base form of bupivacaine. The present disclosure also provides methods for preparing a provided composition, wherein the method comprises: providing an anesthetic; forming a nanoparticle comprising the anesthetic by exposing the anesthetic to a solution of water comprising a protein; and reacting the protein with a crosslinking agent, thereby producing a crosslinked protein matrix. In some embodiments, providing the anesthetic further comprises forming a free base form of the anesthetic. In some embodiments, the free base form of the anesthetic is formed by reacting a salt form of the anesthetic with a base. In some embodiments, the protein is not treated with ethanol prior to reacting with the crosslinking agent. In some embodiments, the protein is not denatured prior to reacting with the crosslinking agent. In some embodiments, the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the protein is bovine serum albumin. In some embodiments, the protein is alpha-1-acid glycoprotein. In some embodiments, the crosslinking agent is of Formula (II): (II), wherein L is optionally substituted alkylene or optionally substituted heteroalkylene. In some embodiments, L is optionally substituted alkylene. In some embodiments, L is optionally substituted C1-12alkylene. In some embodiments, L is optionally substituted C1-6alkylene. In some embodiments, L is optionally substituted C1-3 alkylene. #13447332v2 In some embodiments, L is unsubstituted alkylene. In some embodiments, L is unsubstituted C1-12alkylene. In some embodiments, L is unsubstituted C1-6alkylene. In some embodiments, L is unsubstituted C1-3alkylene. In some embodiments, L is unsubstituted C12alkylene, unsubstituted C11 alkylene, unsubstituted C10 alkylene, unsubstituted C9 alkylene, unsubstituted C8 alkylene, unsubstituted C7 alkylene, unsubstituted C6 alkylene, unsubstituted C5 alkylene, unsubstituted C4alkylene, unsubstituted C3alkylene, unsubstituted C2alkylene, or unsubstituted C1 alkylene. In some embodiments, L is unsubstituted C12 alkylene. In some embodiments, L is unsubstituted C11 alkylene. In some embodiments, L is unsubstituted C10 alkylene. In some embodiments, L is unsubstituted C9alkylene. In some embodiments, L is unsubstituted C8 alkylene. In some embodiments, L is unsubstituted C7 alkylene. In some embodiments, L is unsubstituted C6 alkylene. In some embodiments, L is unsubstituted C5 alkylene. In some embodiments, L is unsubstituted C4alkylene. In some embodiments, L is unsubstituted C3alkylene. In some embodiments, L is unsubstituted C2alkylene. In some embodiments, L is unsubstituted C1 alkylene. In some embodiments, L is methylene, ethylene, n-propylene, isopropylene, n-butylene, tert-butylene, sec-butylene, isobutylene, n-pentylene, 3- pentanylene, amylene, neopentylene, 3-methylene-2-butanylene, tert-amylene, or n-hexylene. In some embodiments, L is methylene, ethylene, n-propylene, n-butylene, n-pentylene, or n- hexylene. In some embodiments, L is methylene. In some embodiments, L is ethylene. In some embodiments, L is n-propylene. In some embodiments, L is n-butylene. In some embodiments, L is n-pentylene. In some embodiments, L is n-hexylene. In some embodiments, the crosslinking agent is glutaraldehyde. In some embodiments, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the crosslinking agent is glutaraldehyde, and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is an anesthetic, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is an anesthetic, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is an anesthetic, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is an anesthetic, the crosslinking agent is #13447332v2 glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is an anesthetic, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is an anesthetic, the crosslinking agent is glutaraldehyde, and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an anesthetic, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an anesthetic, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is a free base form of an anesthetic, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an anesthetic, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of an anesthetic, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is a free base form of an anesthetic, the crosslinking agent is glutaraldehyde, and the protein is alpha-1- acid glycoprotein. In some embodiments, the therapeutic agent is bupivacaine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is bupivacaine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is bupivacaine, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is bupivacaine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is bupivacaine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is bupivacaine, the crosslinking agent is glutaraldehyde, and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of bupivacaine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of bupivacaine, the crosslinking agent is of Formula (II), and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is a free base form of bupivacaine, the crosslinking agent is of Formula (II), and the protein is alpha-1-acid glycoprotein. In some embodiments, the therapeutic agent is a free base form of bupivacaine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin or alpha-1-acid glycoprotein. In some embodiments, the #13447332v2 therapeutic agent is a free base form of bupivacaine, the crosslinking agent is glutaraldehyde, and the protein is bovine serum albumin. In some embodiments, the therapeutic agent is a free base form of bupivacaine, the crosslinking agent is glutaraldehyde, and the protein is alpha-1- acid glycoprotein. The present disclosure also provides compositions prepared by the disclosed methods. EQUIVALENTS AND SCOPE In the claims articles such as “a,” “an,” and “the” may mean one or more than one unless indicated to the contrary or otherwise evident from the context. Claims or descriptions that include “or” between one or more members of a group are considered satisfied if one, more than one, or all of the group members are present in, employed in, or otherwise relevant to a given product or process unless indicated to the contrary or otherwise evident from the context. The invention includes embodiments in which exactly one member of the group is present in, employed in, or otherwise relevant to a given product or process. The invention includes embodiments in which more than one, or all of the group members are present in, employed in, or otherwise relevant to a given product or process. Furthermore, the invention encompasses all variations, combinations, and permutations in which one or more limitations, elements, clauses, and descriptive terms from one or more of the listed claims is introduced into another claim. For example, any claim that is dependent on another claim can be modified to include one or more limitations found in any other claim that is dependent on the same base claim. Where elements are presented as lists, e.g., in Markush group format, each subgroup of the elements is also disclosed, and any element(s) can be removed from the group. It should it be understood that, in general, where the invention, or aspects of the invention, is / are referred to as comprising particular elements and / or features, certain embodiments of the invention or aspects of the invention consist, or consist essentially of, such elements and / or features. For purposes of simplicity, those embodiments have not been specifically set forth in haec verba herein. It is also noted that the terms “comprising” and “containing” are intended to be open and permits the inclusion of additional elements or steps. Where ranges are given, endpoints are included. Furthermore, unless otherwise indicated or otherwise evident from the context and understanding of one of ordinary skill in the art, values that are expressed as ranges can assume any specific value or sub-range within the stated ranges in different embodiments of the invention, to the tenth of the unit of the lower limit of the range, unless the context clearly dictates otherwise. This application refers to various issued patents, published patent applications, journal articles, and other publications, all of which are incorporated herein by reference. If there is a #13447332v2 conflict between any of the incorporated references and the instant specification, the specification shall control. In addition, any particular embodiment of the present invention that falls within the prior art may be explicitly excluded from any one or more of the claims. Because such embodiments are deemed to be known to one of ordinary skill in the art, they may be excluded even if the exclusion is not set forth explicitly herein. Any particular embodiment of the invention can be excluded from any claim, for any reason, whether or not related to the existence of prior art. Those skilled in the art will recognize or be able to ascertain using no more than routine experimentation many equivalents to the specific embodiments described herein. The scope of the present embodiments described herein is not intended to be limited to the above Description, but rather is as set forth in the appended claims. Those of ordinary skill in the art will appreciate that various changes and modifications to this description may be made without departing from the spirit or scope of the present invention, as defined in the following claims. EXAMPLES In order that the disclosure described herein may be more fully understood, the following examples are set forth. The examples described in this application are offered to illustrate the compounds, pharmaceutical compositions, and methods provided herein and are not to be construed in any way as limiting their scope. Synthesis and characterization of BNP@BSA-X A glutaraldehyde-crosslinked bovine serum albumin hydrogel (BSA-X) containing bupivacaine free base nanoparticles (BNPs), abbreviated BNP@BSA-X, was made by a one-pot approach (FIG.1). In brief (see Methods) the free base of bupivacaine was produced by alkaline precipitation of bupivacaine hydrochloride. The free base was then dissolved in methanol and introduced dropwise into bovine serum albumin (BSA) in phosphate-buffered saline (PBS) at pH 7.4, yielding bupivacaine nanoparticles (BNP) within BSA (BNP@BSA). The methanol was evaporated by rotary evaporation. Finally, glutaraldehyde (GA) was added to crosslink the BSA and form a BSA hydrogel with embedded BNPs (BNP@BSA-X). The hydrodynamic diameter of BNPs in BSA prior to crosslinking was ~190 nm by dynamic light scattering (DLS) (FIG.2A), with a narrow size distribution. There was also a population of ~7 nm NPs, corresponding to BSA protein. After washing to remove excess BSA, BNP@BSA measured 70-100 nm by transmission electron microscopy (TEM; FIG.2B). The discrepancy between diameters by TEM and DLS is because the latter measures the hydrodynamic diameter. #13447332v2 BNP@BSA-X was synthesized using 50 mg / ml or 100 mg / ml of BSA and 5 mg / ml or 10 mg / ml of GA. In contrast to BNP in PBS and BNP@BSA, which remained in a liquid state, all BNP@BSA-X samples formed hydrogels (FIG.8). The gelation time (the time after the addition of GA for storage moduli to plateau) was shorter with 100 mg / ml BSA than 50 mg / ml BSA (FIG.9). The BNP@BSA-X hydrogels had a storage modulus (G') greater than the loss modulus (G'') at all concentrations of BSA and GA, indicating solid-like properties (FIG.10). The higher GA concentration (10 mg / ml) resulted in a higher G' (FIGs.2C and 10), likely due to increased crosslinking between BSA proteins. Since all the BNP@BSA-X formed hydrogels, 50 mg / ml BSA (with 5 or 10 mg / ml of GA) was used in downstream experiments, to minimize the mass to be injected in vivo. The design is of drug nanoparticles contained within a cross-linked albumin hydrogel. Cross-linking would occur prior to administration a) to ensure that the cross-linking occurs within the drug delivery system rather than with tissues, b) to minimize the extent to which the system will dissipate after injection, and c) to reduce the need for rapid cross-linking in vivo. For this purpose, it would be desirable to have shear-thinning properties, i.e., for the material to be highly elastic prior to injection, be readily injectable, then to regain elasticity after injection. The mechanical properties of BNP@BSA-X formulations were evaluated by rheometry through step-strain oscillations (FIGs.2D and 11). For BNP@BSA-X (5 mg / ml GA), the application of strain (500%) led to liquid-like properties, with G' < G'' (FIG.2D). Upon the removal of excess strain (0.1%), G' exceeded G'' within seconds. During repeated cycles, full or near-complete healing was achieved. BNP@BSA-X (10 mg / ml GA) exhibited a decrease in G' with repeated strain cycles at 0.1% (FIG.11). When exposed to a high strain of 500%, G' closely approached G'', suggesting a lack of shear-thinning behavior. BNP@BSA with 10 mg / ml GA was difficult to inject through a 23-gauge needle. BNP@BSA-X with 50 mg / ml BSA and 5 mg / ml GA was used in downstream studies. Scanning electron microscopy of BNP@BSA-X showed a pore size of approximately 5- 10 μm, suggesting a large surface area and high water-absorption capacity (FIG.12). The release of bupivacaine from formulations containing bupivacaine•HCl was similar to that of bupivacaine•HCl (for the comparison of the latter to bupivacaine•HCl@BSA at 24h, p = 0.18; to bupivacaine•HCl@BSA-X; p = 0.54) (FIG.2E). In contrast, the release of bupivacaine from BNP was slower from bupivacaine•HCl (p=0.0005 at 24 hr). The hydrophobic nature of the free base, and the lower surface area / volume ratio of BNP compared to the free drug could have contributed to the slower release. #13447332v2 Bupivacaine release from BNP@BSA and BNP@BSA-X were much slower than from BNP in PBS (both p<0.0001 at 24 hr), underscoring the significant role of BSA in slowing release. The release kinetics of BNP@BSA and BNP@BSA-X were similar (p=0.085 at 24 hr). This similarity in vitro could be due the fact that the dialysis device physically constrained the BSA solution within a fixed volume at the same concentration as BSA-X, i.e., mimicking a cross-linked hydrogel. While the interaction between bupivacaine and serum albumin has been studied, the interaction between BNP and serum albumin has not been reported. The interaction between BNP and BSA was investigated by measuring their fluorescence and UV-Vis spectra (FIGs.16- 17). Upon adding BNP (0.05, 0.1, and 0.2 mg / ml) to the 1 mg / ml BSA solution, there was quenching of the emission peak of BSA at around 335 nm upon excitation at 280 nm (FIG.16). This peak is associated with the intrinsic fluorescence of tryptophan residues in BSA. The observed quenching suggests potential molecular interactions, possibly induced by energy transfer or molecular rearrangement of BSA. BNP alone in PBS did not show any emission in this wavelength range upon the same excitation, indicating that these changes in spectra are related to BSA. UV-Vis absorption studies revealed a shift in the spectra of BSA around 260 nm with introduction of BNP (FIG.17). This shift can be attributed to the π → π* transition of aromatic amino acids, including Trp, Tyr, and Phe in BSA. Additionally, alterations in the spectra of BSA in the 210-230 nm range indicated changes in the structural conformation of BSA following the addition of BNP. The BNP alone in PBS did not show distinct absorbance in this range of wavelengths, demonstrating that these absorbance changes are related to structural changes in BSA. Release of other compounds To illustrate the broader applicability of this approach to different drugs, diphenhydramine, an antihistamine, was used as an example of an amphiphilic drug (water solubility : 683 mg / ml, log P: 3.06), and paclitaxel was used as a hydrophobic chemotherapy drug (water solubility<0.1ug / ml, log P: 3.20) (FIGs.3 and 13A-13C). Nanoparticles were prepared from both drugs and incorporated into crosslinked BSA. In brief, the free base form of diphenhydramine was generated by adding triethylamine (TEA) to diphenhydramine•HCl in methanol then added dropwise to a 50 mg / ml BSA solution in pH 7.4 PBS. After evaporating the methanol, glutaraldehyde (GA) was added to crosslink the BSA, forming diphenhydramine nanoparticles in crosslinked BSA (DHNP@BSA-X). Paclitaxel was dissolved in methanol and added to a 50 mg / ml BSA solution in pH 7.4 PBS. Methanol was evaporated, then GA was #13447332v2 added to create paclitaxel nanoparticles in crosslinked BSA (PNP@BSA-X). Release from DHNP@BSA-X and PNP@BSA-X was significantly slower than that of the respective free drugs (p<0.0001 at 24 hr). Sciatic nerve blockade Various formulations (0.3 ml) were injected at the left sciatic nerve of rat subjects, and neurobehavioral testing was conducted to evaluate the duration of sensory and motor functional deficits, in both hind paws (FIGs.4 and 14A-14B). Deficits in the left (injected) hindpaw reflect nerve block, while deficits in the right (uninjected) hindpaw reflect effects of systemically distributed bupivacaine. None of the formulations caused deficits in the uninjected hindpaw throughout the study (FIG.19). Bupivacaine at 5 mg / ml – 0.5% v / w achieved a sensory block duration of 2.6 h (FIG.4). Block from 5 mg / ml BNP in uncrosslinked BSA (BNP@BSA) lasted 2.5 h (p=0.827 compared to free bupivacaine). The duration of sensory block from BNP@BSA increased with increasing bupivacaine nanoparticle concentration (2.9 hr for 10 mg / ml and 3.8 hr for 20 mg / ml), but the increase was not statistically significant, and reached a maximum duration of approximately 4 hr. Cross-linking the BSA (BNP@BSA-X) markedly increased the duration of block at every bupivacaine loading; the durations of block were 4.2 (5 mg / ml; p = 0.077), 6.4 (10 mg / ml; p= 0.011), and 10.6 (20 mg / ml; p<0.0001) fold longer with cross-linked than non-cross-linked BSA, respectively. At 20 mg / ml bupivacaine, BNP@BSA-X achieved 39.9 h of nerve block. By way of comparison, the duration achieved by the same volume of commercially available 13.3 mg / ml bupivacaine liposomes (Exparel®) was 5.1 h, i.e., 8-fold shorter (p<0.0001). Sensory nerve block with 20 mg / ml bupivacaine•HCl@BSA-X (7.3 hr) was 5.4-fold shorter than with BNP@BSA-X (39.9 hr, p<0.0001). This observation aligns with in vitro release kinetics (FIG.2E). There was no difference in the durations of sensory and motor block in any formulation (FIGs.14A-14B). In the absence of bupivacaine, BSA and BSA-X did not cause nerve block. Tissue retention To evaluate drug retention in tissue, the hydrophobic near-infrared (NIR) dye indocyanine green (ICG) was used as a model drug (excitation 790 nm, emission 810 nm). Nanoparticles containing ICG and bupivacaine (ICG-BNP) were formed by the same process as for BNP except that ICG was co-dissolved in methanol with bupivacaine. When free ICG and ICG-BNP@BSA were injected at the sciatic nerve of rat subjects (FIGs.5A-5B), the associated fluorescence became undetectable within 24 hr. Cross-linking of the BSA markedly enhanced retention of ICG. With cross-linked BSA, release of ICG incorporated in BNP (ICG- #13447332v2 BNP@BSA-X) was slower than from bupivacaine•HCl in PBS (ICG-bupivacaine•HCl@BSA- X) (51% vs.82 % respectively at 28 days, p = 0.006). These data suggest that both nanoformulation and the cross-linking of BSA contributed to prolonging retention in tissue. To track tissue retention of BSA-X, the dye Cy5.5 was covalently bound to BSA (Cy5.5- BSA; excitation 660 nm, emission 710 nm). When free Cy5.5 or non-cross-linked cy5.5-BSA containing BNP (BNP@Cy5.5-BSA) was injected at the sciatic nerve, the associated fluorescence decreased by approximately 80% within 7 days. In contrast, when BSA was crosslinked (BNP@Cy5.5-BSA-X), the fluorescence decreased by 36.2% over the same period (p= 0.004 when comparing to free Cy5.5 and p=0.005 when comparing to BNP@Cy5.5-BSA; FIGs.5C-5D). The duration of the nerve block from formulations correlated with the half-life of tissue retention of the model drug ICG, calculated from data in FIG.5B (FIG.6A) (the half-life is time to a 50% reduction in fluorescence relative intensity.). The durations of nerve block and tissue retention from bupivacaine•HCl@BSA-X were much shorter than from BNP@BSA-X, supporting the benefit of nanoformulation. The duration of nerve block and tissue retention from crosslinked BSA (BNP@BSA-X and bupivacaine•HCl@BSA-X) were much longer than from non-crosslinked BSA (BNP@BSA), indicating the significance of BSA cross-linking. The duration of nerve block also correlated with the percentage of fluorescence relative intensity of Cy5.5 dye remaining on day 2 (FIG.6B), as calculated from data in FIG.5D. In particular, cross-linking of BSA (BNP@BSA-X vs. BNP@BSA) was associated with much longer duration of block. These correlations are consistent with the attribution of the similarity of the release of bupivacaine from BNP@BSA and BNP@BSA-X in vitro (FIG.2E) to restriction of the diffusion of BSA. Tissue reaction Tissue reaction was assessed 4 days after the injection of BNP@BSA-X (20 mg / mL bupivacaine) in rat subjects, a time frame when acute inflammation and muscle injury are typically well-established following perineural injection of drugs and biomaterials (FIGs.7A- 7E). The sciatic nerves and adjacent tissues were harvested, processed into hematoxylin-eosin (H&E) stained sections and inflammation and myotoxicity were assessed (inflammation scores 0-4; myotoxicity scores 0-6). In all rats treated with BNP@BSA-X, discrete eosinophilic deposits (indicating protein) were found in close proximity to the sciatic nerve (FIG.7A). On histological examination, the response to BNP@BSA-X was characterized by a mixed inflammatory infiltrate primarily composed of macrophages, along with a smaller population of lymphocytes and occasional neutrophils in the soft tissues surrounding the muscle #13447332v2 (inflammation; median score: 2). Furthermore, evidence of myotoxicity induced by BNP@BSA- X was observed, with degenerating and regenerating myocytes predominantly located in the perifascicular region of the muscle bundle (myotoxicity; median score: 1). Injection of the same volume of the commercially available EXPAREL®(bupivacaine concentration 13.3 mg / mL), had a similar level of inflammation (median score: 2, p = 0.5) but had more myotoxicity (median score: 3, p = 0.019). In sustained release systems for conventional local anesthetics, the biomaterial and the drugs can cause inflammation which lasts as long as there is residual material present. The inflammation resolves completely when both are gone, with no apparent sequelae. The local anesthetic itself can also cause myotoxicity, which also resolves completely once the drug is gone. This resolution was verified through histological examination conducted 30 days post- injection of BNP@BSA-X (FIGs.18A-18B). Discussion Presented herein is the development of an injectable depot platform of drug nanoparticles within a protein-based hydrogel system that is formed by a one-pot synthesis that does not require additional purification steps. This platform can achieve prolonged delivery of diagnostic and therapeutic agents (e.g., local anesthetics, antihistamines, chemotherapeutics). In an embodiment, the strategy involves forming bupivacaine nanoparticles using the hydrophobic free base form of bupivacaine, which are then stabilized with BSA proteins. In another embodiment, the strategy involves forming diphenhydramine nanoparticles using the hydrophobic free base form of diphenhydramine, which are then stabilized with BSA proteins. In another embodiment, the strategy involves forming paclitaxel nanoparticles, which are then stabilized with BSA proteins. The resulting nanoparticles are then crosslinked to create a stiff protein hydrogel. The protein (e.g., BSA) plays a crucial role in this process, facilitating the stabilization of nanoparticles while also serving as a matrix for the production of hydrogel. This system offers the advantage of dose flexibility for the drug. If the solvent used for drug dissolution, in this case, methanol, does not reach its saturation limit, it permits a significant increase in drug dosage. This flexibility can be particularly beneficial, especially when local anesthesia is needed for larger animals, where the minimum effective dose is higher. Additionally, this approach presents an advantage over other drug delivery systems that involve drug encapsulation, as they impose limitations on drug doses due to purification or synthesis steps. For in vivo demonstration of safety and efficacy, a sciatic nerve blockade in rat subjects was evaluated with bupivacaine, a relatively long-acting local anesthetic. The nanoparticulate #13447332v2 and cross-linked protein components were both involved in achieving prolonged nerve block. The nanoparticulate contribution may be due to the fact that the bupivacaine was in hydrophobic free base form, which would slow diffusion away from the depot. BSA slowed release by binding of bupivacaine. Drug binding to BSA may have had a greater effect than cross-linking per se, as evidenced by the fact that bupivacaine release was similar for BNP@BSA and BNP@BSA-X in vitro, i.e., when diffusion / dilution of BSA was prevented by containment within a dialysis membrane. However, BNP@BSA-X resulted in much longer block durations than BNP@BSA in vivo, where disappearance of BSA from the site of injection was not limited. Moreover, the micron-scale pore size of BSA-X is unlikely to have a marked effect on diffusion of bupivacaine. This view is supported by the experience with cross-linked hyaluronic acid hydrogels, which had a relatively modest effect on the release and duration of block from bupivacaine hydrochloride, and had a similar pore size to BSA-X. Injectable drug delivery systems almost invariably entail local inflammation. When used to deliver conventional local anesthetics, myotoxicity also occurs. Although such injury often recovers spontaneously, it is not desirable and can result in serious injury. At high concentrations of local anesthetics or particularly toxic agents, there can be nerve injury. The concentration of local anesthetic is a primary determinant of tissue injury. Tissue reaction can be a limiting factor with sustained release systems for conventional local anesthetics, preventing the achievement of very long block. In the present disclosure, nerve block from BNP@BSA-X lasted 8 times longer than block from Exparel®(13.3 mg / ml bupivacaine), a commercially available liposomal bupivacaine product, and had comparable or superior tissue reaction, even though it contained more bupivacaine (20 mg / ml). Moreover, none of the animals tested had neurobehavioral deficits in the contralateral (un-injected) hindpaw, suggesting that there was no effect from systemically distributed drug. This is important because of the potential for systemic toxicity with conventional local anesthetics. These data suggest that the approach described herein can provide safe prolonged local anesthesia, and can be used for the prolonged delivery of other drugs of other drugs, such as antihistamines and chemotherapeutics. Methods Reagents All materials and reagents, unless otherwise noted, were purchased from Sigma-Aldrich (St. Louis, MO, USA), and used as received. Synthesis of Bupivacaine free base Bupivacaine hydrochloride was dissolved in 50 mL of deionized water, and a 0.2M NaOH solution was slowly added under stirring. The free base form began to precipitate as a #13447332v2 white solid, and the NaOH solution was continuously added until a pH of 11 was achieved (pKa = 8.4). The resulting white solid was filtered under vacuum and washed with deionized water multiple times. The solid was subsequently dried under vacuum overnight. General method to prepare BSA gel (BSA-X) 500 mg / ml glutaraldehyde solution (GA) was added to the stirring BSA protein solution to achieve the desired final concentration of 5 mg / mL or 10 mg / mL GA. Preparation of BNP in BSA-X (BNP@BSA-X) Bupivacaine free base was dissolved in methanol to prepare a stock solution. Bovine serum albumin (BSA) was dissolved in pH 7.4 phosphate-buffered saline (PBS). The BSA solution was vigorously stirred while rapidly adding the bupivacaine free base solution. Adding bupivacaine free base directly to PBS without BSA resulted in immediate aggregation (FIG.15). The resulting mixture was then subjected to rotary evaporation to remove the methanol and continuously stirred for 2 hours to promote the hardening of nanoparticles (BNP@BSA). Subsequently, glutaraldehyde (GA) was added to the solution at a final concentration of 5 mg / ml or 10 mg / ml to create the bupivacaine nanoparticle-embedded hydrogel, denoted as BNP@BSA- X. Preparation of DHNP in BSA-X(DHNP@BSA-X) Diphenhydramine hydrochloride was dissolved in methanol at a concentration of 100 mg / ml, and triethylamine (TEA) was added at a volume ratio of 1% (v / v). After 30 minutes of stirring, this solution was introduced into the BSA solution, previously prepared in pH 7.4 PBS at a concentration of 50 mg / ml. This addition resulted in a final diphenhydramine concentration of 1 mg / ml. Subsequently, GA was added to the solution at a final concentration of 5 mg / ml to create the diphenhydramine nanoparticle-embedded hydrogel, denoted as DHNP@BSA-X. Preparation of PNP in BSA-X(BNP@BSA-X) Paclitaxel was dissolved in methanol to create a stock solution with a concentration of 100 mg / ml. Concurrently, bovine serum albumin (BSA) was dissolved in pH 7.4 phosphate- buffered saline (PBS) at a concentration of 50 mg / ml. The BSA solution was vigorously stirred while the paclitaxel solution was rapidly added to reach a final paclitaxel concentration of 1 mg / ml. The resulting mixture underwent rotary evaporation to remove the methanol and was continuously stirred for 2 hr to facilitate nanoparticle hardening. Subsequently, GA was added to the solution at a final concentration of 5 mg / ml to create the paclitaxel nanoparticle-embedded hydrogel, denoted as PNP@BSA-X. #13447332v2 Preparation of bupivacaine•HCl in BSA (Bupivacaine•HCl@BSA) To prepare bupivacaine•HCl in BSA (Bupivacaine•HCl@BSA), the bupivacaine•HCl was dissolved in water, and then a solution of BSA in a pH 7.4 buffer was added to the mixture. The resulting mixture was then stirred to create Bupivacaine•HCl@BSA. Preparation of ICG and BNP in BSA (ICG-BNP@BSA) A stock solution was prepared by dissolving ICG (0.5 mg / ml) and Bupivacaine free base (200 mg / ml) in methanol. In a separate solution, bovine serum albumin (BSA) (50 mg / ml) was dissolved in pH 7.4 phosphate-buffered saline (PBS) and vigorously stirred. The Bupivacaine free base and ICG solution were then rapidly added to the BSA solution while stirring. The final concentration of BNP and ICG was 20 mg / ml and 0.05 mg / ml, respectively. The resulting mixture was subjected to rotary evaporation to remove the methanol and continuously stirred for 2 hours to promote the hardening of nanoparticles. Preparation of ICG and bupivacaine•HCl in BSA hydrogel (ICG-Bupivacaine•HCl @BSA-X) To prepare ICG and bupivacaine•HCl in BSA, a solution was created by dissolving both ICG and bupivacaine•HCl in BSA solution. The resulting solution was then treated with addition of a 500 mg / ml glutaldehyde solution to achieve the desired final concentration of 5 mg / ml. Preparation of BNP in Cy5.5 dye conjugated BSA hydrogel (BNP@Cy5.5-BSA-X) Bupivacaine free base was dissolved in methanol to prepare a stock solution. Then, a solution of Cy5.5 dye-conjugated BSA (Cy5.5-BSA, purchased from Nanocs Inc, New York, NY, USA) was mixed with BSA to create a mixture with a final concentration of 50 mg / ml BSA. The concentration of Cy5.5 dye in the solution was 0.05 mg / ml. The mixture was vigorously stirred while the bupivacaine free base was rapidly added. The resulting mixture was then subjected to rotary evaporation to remove the methanol and continuously stirred for 2 hours to promote the hardening of nanoparticles. The resulting solution was then treated with addition of a 500 mg / ml glutaraldehyde solution to achieve the desired final concentration of 5 mg / ml. Dynamic Light Scattering (DLS) The particle size was measured with a Malvern Nano ZetaSizer (Malvern Panalytical, Westborough, MA, USA). Transmission Electron Microscopy (TEM) The BNP@BSA solution was prepared by subjecting it to centrifugation to remove any excess BSA protein. The resulting pellet was then washed three times and resuspended in water. Carbon-coated 400 mesh copper grids (Ted Pella, Inc., Redding, CA, USA) were subjected to #13447332v2 glow charging for 90 seconds before BNP@BSA solution were deposited on them. A volume of 5 μL of resuspended BNP@BSA was placed on the grid and allowed to settle for 5 minutes. The grid was then washed with distilled water, stained with 1% (w / w) uranyl acetate, and wicked dry with filter paper. Transmission electron microscopy (TEM) images were acquired using a Tecnai G2 Spirit BioTWIN transmission electron microscope (FEI company, Hillsboro, OR, USA) operating at an acceleration voltage of 80 kV. Scanning electron microscope (SEM) The surface morphology of the hydrogel was examined using a Hitachi S-4700 Field Emission Scanning Electron Microscope (FE-SEM) at an accelerating voltage of 10 kV and 12 μA. The BSA hydrogel was prepared, flash-frozen in liquid nitrogen, and subsequently lyophilized. Prior to imaging, the sample cross-sections were obtained using a razor blade and mounted on SEM stubs with double-sided carbon tape. To enhance conductivity, the samples were further coated with an Au / Pd alloy using sputter coating techniques. Rheological testing The rheological characteristics of the formulations were evaluated by means of a TA DHR-2 rheometer (TA instruments, NewCastle, DE, USA) furnished with a temperature regulator. A parallel plate with a diameter of 20 mm was implemented in all tests. The distance between the plates was set at 0.3 mm. The gelation time was recorded over a 5-hour period at a frequency of 6.28 rad / s and a strain of 0.1%. Frequency sweeps were conducted within the range of 0.63 to 628 rad / s with a strain of 0.1%. Step-strain oscillation tests we...

Claims

CLAIMS What is claimed is:

1. A composition comprising a hydrogel and a protein-stabilized nanoparticle, wherein: the hydrogel comprises a crosslinked protein matrix; the protein-stabilized nanoparticle comprises a therapeutic agent or a diagnostic agent; and the protein-stabilized nanoparticle is embedded in the crosslinked protein matrix.

2. A composition comprising a hydrogel and a nanoparticle, wherein: the hydrogel comprises a crosslinked protein matrix; the nanoparticle comprises an anesthetic; and the nanoparticle is embedded in the crosslinked protein matrix.

3. The composition of claim 1, wherein the crosslinked protein matrix comprises a crosslinked protein.

4. The composition of any of the preceding claims, wherein the crosslinked protein is crosslinked bovine serum albumin.

5. The composition of any of the preceding claims, wherein the crosslinked protein matrix is covalently crosslinked.

6. The composition of any of the preceding claims, wherein the crosslinked protein matrix comprises a moiety of Formula (I): wherein:each instance of Z is independently a protein in the crosslinked protein matrix; and L is optionally substituted alkylene or optionally substituted heteroalkylene.

7. The composition of any of the preceding claims, wherein L is unsubstituted C1-12alkylene. #13447332v28. The composition of any of the preceding claims, wherein the crosslinked protein matrix comprises a moiety of formula: ,wherein each instance of Z is a crosslinked protein matrix.

9. The composition of any of the preceding claims, wherein at least one instance of Z is bovine serum albumin.

10. The composition of any of the preceding claims, wherein the hydrogel comprises pH 7.4 phosphate-buffered saline (PBS).

11. The composition of any of the preceding claims, wherein the protein-stabilized nanoparticle comprises a hydrodynamic diameter of between about 100 nm and about 400 nm, between about 100 nm and about 300 nm, between about 100 nm and about 200 nm, between about 200 nm and about 300 nm, between about 125 nm and about 300 nm, between about 125 nm and about 275 nm, between about 125 nm and about 250 nm, between about 125 nm and about 225 nm, between about 150 nm and about 300 nm, between about 150 nm and about 275 nm, between about 150 nm and about 250 nm, between about 150 nm and about 225 nm, between about 175 nm and about 300 nm, between about 175 nm and about 275 nm, between about 175 nm and about 250 nm, or between about 175 nm and about 225 nm.

12. The composition of any of the preceding claims, wherein the protein-stabilized nanoparticle comprises a hydrodynamic diameter of about 200 nm.

13. The composition of any of the preceding claims, wherein the protein-stabilized nanoparticle is not covalently attached to the hydrogel.

14. The composition of any of the preceding claims, wherein the protein-stabilized nanoparticle is not covalently attached to the crosslinked protein matrix.

15. The composition of any of the preceding claims, wherein the nanoparticle comprises a hydrodynamic diameter of between about 100 nm and about 400 nm, between about 100 nm and about 300 nm, between about 100 nm and about 200 nm, between about 200 nm and about 300 #13447332v2nm, between about 125 nm and about 300 nm, between about 125 nm and about 275 nm, between about 125 nm and about 250 nm, between about 125 nm and about 225 nm, between about 150 nm and about 300 nm, between about 150 nm and about 275 nm, between about 150 nm and about 250 nm, between about 150 nm and about 225 nm, between about 175 nm and about 300 nm, between about 175 nm and about 275 nm, between about 175 nm and about 250 nm, or between about 175 nm and about 225 nm.

16. The composition of any of the preceding claims, wherein the nanoparticle comprises a hydrodynamic diameter of about 200 nm.

17. The composition of any of the preceding claims, wherein the nanoparticle is not covalently attached to the hydrogel.

18. The composition of any of the preceding claims, wherein the nanoparticle is not covalently attached to the crosslinked protein matrix.

19. The composition of any of the preceding claims, wherein the crosslinked protein matrix is prepared by reacting a protein with a crosslinking agent.

20. The composition of any of the preceding claims, wherein the protein is not treated with ethanol prior to reacting with the crosslinking agent.

21. The composition of any of the preceding claims, wherein the protein is bovine serum albumin or alpha-1-acid glycoprotein.

22. The composition of any of the preceding claims, wherein the protein is bovine serum albumin.

23. The composition of any of the preceding claims, wherein the crosslinking agent comprises two acyl groups.

24. The composition of any of the preceding claims, wherein the crosslinking agent is of formula: , #13447332v2wherein L is optionally substituted alkylene or optionally substituted heteroalkylene.

25. The composition of any of the preceding claims, wherein L is unsubstituted C1-12alkylene.

26. The composition of any of the preceding claims, wherein the crosslinking agent is glutaraldehyde.

27. The composition of any of the preceding claims, wherein the bovine serum albumin is present in a concentration of between about 50 mg / mL and about 100 mg / mL.

28. The composition of any of the preceding claims, wherein the glutaraldehyde is present in a concentration of between about 5 mg / mL and about 10 mg / mL.

29. The composition of any of the preceding claims, wherein the bovine serum albumin is present in a concentration of about 50 mg / mL, and the glutaraldehyde is present in a concentration of about 5 mg / mL.

30. The composition of any of the preceding claims, wherein the therapeutic agent is an anesthetic.

31. The composition of any of the preceding claims, wherein the therapeutic agent is a free base form of an anesthetic.

32. The composition of any of the preceding claims, wherein the therapeutic agent is a local anesthetic.

33. The composition of any of the preceding claims, wherein the therapeutic agent is a site 1 sodium channel blocker, amino ester local anesthetic, or an amino amide local anesthetic.

34. The composition of any of the preceding claims, wherein the therapeutic agent is a small molecule.

35. The composition of any of the preceding claims, wherein the therapeutic agent is tetrodotoxin, saxitoxin, neosaxitoxin, bupivacaine, amylocaine, ambucaine, articaine, #13447332v2benzocaine, benzonatate, butacaine, butanilicaine, carbocaine, cepastat, chloraseptic, chloroprocaine, cinchocaine, citanest, cyclomethycaine, dibucaine, diperodon, dimethocaine, eucaine, etidocaine, fomocaine, fotocaine, hydroxyprocaine, isobucaine, levobupivacaine, lidocaine, marcaine, mepivacaine, meprylcaine, metabutoxycaine, nitracaine, orthocaine, orabloc, oxetacaine, oxybuprocaine, paraethoxycaine, phenacaine, piperocaine, piridocaine, polocaine, posimir, pramocaine, prilocaine, primacaine, procaine, procainamide, proparacaine, propoxycaine, pyrrocaine, quinisocaine, ropivacaine, sensorcaine, septocaine, trimecaine, tetracaine, tolycaine, tropacocaine, ulcerease, xylocaine, zorcaine, decarbamoyl saxitoxin, gonyautoxins, or derivatives thereof.

36. The composition of any of the preceding claims, wherein the therapeutic agent is bupivacaine.

37. The composition of any of the preceding claims, wherein the therapeutic agent is bupivacaine present in the composition in a concentration of about 20 mg / mL.

38. The composition of any of the preceding claims, wherein the therapeutic agent is hydrophobic.

39. The composition of any of the preceding claims, wherein the therapeutic agent does not comprise a primary or secondary amine.

40. The composition of any of the preceding claims, wherein the therapeutic agent is an anti- cancer agent or an antihistamine.

41. The composition of any of the preceding claims, wherein the therapeutic agent is a free base form of an anti-cancer agent or an antihistamine.

42. The composition of any of the preceding claims, wherein the therapeutic agent is paclitaxel or diphenhydramine.

43. The composition of any of the preceding claims, wherein the therapeutic agent is a free base form of paclitaxel or diphenhydramine. #13447332v244. The composition of any of the preceding claims, wherein the therapeutic agent is not doxorubicin.

45. The composition of any of the preceding claims, further comprising a pharmaceutically acceptable excipient.

46. The composition of any of the preceding claims, wherein the composition is characterized in that, when tested in vitro by placing the composition in a medium, less than about 100%, less than about 90%, less than about 80%, less than about 70%, less than about 60%, less than about 50%, less than about 40%, less than about 30%, less than about 20%, or less than about 10% of the therapeutic agent is released from the composition 24 hours after placing the composition in the medium.

47. The composition of any of the preceding claims, wherein the composition is characterized in that, when administered to a subject, less than about 100%, less than about 90%, less than about 80%, less than about 70%, less than about 60%, less than about 50%, less than about 40%, less than about 30%, less than about 20%, or less than about 10% of the therapeutic agent is released from the composition 24 hours after administration of the composition.

48. The composition of any of the preceding claims, wherein the composition is characterized in that, when administered to a subject, duration of a therapeutic effect is extended by at least about 10%, at least about 20%, at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, at least about 90%, at least about 100%, or at least about 200% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not the composition of any of the preceding claims.

49. The composition of any of the preceding claims, wherein the therapeutic effect is nerve block and / or reduced pain.

50. The composition of any of the preceding claims, wherein the therapeutic effect is sciatic nerve block. #13447332v251. The composition of any of the preceding claims, wherein the composition exhibits a honeycomb-like structure with pores having a diameter of between about 5 μm and about 10 μm in size.

52. The composition of any of the preceding claims, wherein the composition comprises a storage modulus (G′) that is greater than a loss modulus (G′′) at a temperature of about 25 ℃.

53. The composition of any of the preceding claims, wherein the composition is injectable.

54. The composition of any of the preceding claims, wherein the composition is biodegradable.

55. A method for preparing the composition of any of the preceding claims, wherein the method comprises: providing a therapeutic agent or a diagnostic agent; forming a protein-stabilized nanoparticle comprising the therapeutic agent or the diagnostic agent by exposing the therapeutic agent or the diagnostic agent to a solution of a protein in water; and reacting the protein with a crosslinking agent, thereby producing a crosslinked protein matrix.

56. The method of any of the preceding claims, wherein providing the therapeutic agent or the diagnostic agent further comprises forming a free base form of the therapeutic agent or the diagnostic agent.

57. The method of any of the preceding claims, wherein the free base form of the therapeutic agent or the diagnostic agent is formed by reacting a salt form of the therapeutic agent or the diagnostic agent with a base.

58. A method for preparing the composition of any of the preceding claims, wherein the method comprises: providing an anesthetic; forming a nanoparticle comprising the anesthetic by exposing the anesthetic to a solution of water comprising a protein; and #13447332v2reacting the protein with a crosslinking agent, thereby producing a crosslinked protein matrix.

59. The method of any of the preceding claims, wherein providing the anesthetic further comprises forming a free base form of the anesthetic.

60. The method of any of the preceding claims, wherein the free base form of the anesthetic is formed by reacting a salt form of the anesthetic with a base.

61. A composition prepared by the method of any one of the preceding claims.

62. A method of treating a disease or condition, the method comprising administering an effective amount of the composition of any of the preceding claims to a subject in need thereof.

63. The method of any of the preceding claims, wherein less than about 100%, less than about 90%, less than about 80%, less than about 70%, less than about 60%, less than about 50%, less than about 40%, less than about 30%, less than about 20%, or less than about 10% of the therapeutic agent is released from the composition 24 hours after administration of the composition to the subject.

64. The method of any of the preceding claims, wherein duration of a therapeutic effect is extended by at least about 10%, at least about 20%, at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, at least about 90%, at least about 100%, at least about 200%, at least about 300%, at least about 400%, at least about 500%, at least about 600%, at least about 700%, at least about 800%, at least about 900%, at least about 1,000%, or at least about 10,000% compared to duration of a therapeutic effect upon administration of the therapeutic agent alone or in a composition that is not the composition of any of the preceding claims.

65. The method of any of the preceding claims, wherein the therapeutic effect is nerve block and / or reduced pain.

66. The method of any of the preceding claims, wherein the therapeutic effect is sciatic nerve block. #13447332v267. The method of any of the preceding claims, wherein the disease or condition is pain.

68. The method of any of the preceding claims, wherein the subject is a mammal.

69. The method of any of the preceding claims, wherein the subject is a human. #13447332v2

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