WO2024172859A1 - Peptide formulations - Google Patents

Abstract

Described herein are peptide formulations and methods of making and using the same.

Description

Attorney Docket No.55002-0003WO1 PEPTIDE FORMULATIONS CLAIM OF PRIORITY This application claims the benefit of U.S. Provisional Application Serial No. 63/446,565, filed on February 17, 2023. The entire contents of the foregoing are incorporated herein by reference. SEQUENCE LISTING This application contains a Sequence Listing that has been submitted electronically as an XML file named “55002-0003WO1_SL_ST26.XML.” The XML file, created on August 16, 2023, is 19,379 bytes in size. The material in the XML file is hereby incorporated by reference in its entirety. TECHNICAL FIELD The present application relates to peptide formulations and methods of making and using the same. BACKGROUND Peptide therapies offer significant promise, but are often difficult to formulate. The present application addresses these and other deficiencies in the art. SUMMARY Described herein are, among other things, new peptide formulations, and methods of manufacturing the same. The formulations described herein can be manufactured in a robust and scalable manner, without the difficulties associated with prior formulations (e.g., as described herein). And, as an additional surprising and unexpected benefit, the formulations described herein have remarkably improved stability, even at accelerated conditions (room temperature and above). The peptides described herein can replace therapies that are prohibitively expensive, addictive, and/or invasive. Formulations of the peptide that can be manufactured in a robust and scalable manner, and that are highly stable even under non-refrigeration conditions allow clinicians, medical professionals, laboratory personnel, and researchers to produce amounts of therapeutic peptides for administration to patients in need thereof. Attorney Docket No.55002-0003WO1 Thus, provided herein are lyophilized compositions comprising: a peptide comprising or consisting of the amino acid sequence SGLPDLKLLQVVYLHSNNI (SEQ ID NO: 20) or fragment thereof (e.g., 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, or 18 consecutive amino acids of SEQ ID NO: 20), optionally with one or more conservative amino acid substitutions, or a salt thereof, optionally a pharmaceutically acceptable salt; and a bulking agent. In some embodiments, the peptide or pharmaceutically acceptable salt thereof comprises or consists of the amino acid sequence L-X1-V-V-X2-L-X3, (SEQ ID NO: 1), where X1 is Q or N; X2 is Y, F, or W; X3 is H, K, or R; L is Leucine; Q is Glutamine, N is Asparagine, V is Valine, Y is Tyrosine, F is Phenylalanine, W is Tryptophan, H is Histidine, K is Lysine, and R is Arginine. In some embodiments, the peptide comprises or consists of an amino acid sequence selected from the group consisting of LQVVYLH (SEQ ID NO: 2), LQVVYLK (SEQ ID NO: 3), LQVVYLR (SEQ ID NO: 4), LQVVFLH (SEQ ID NO: 5), LQVVFLK (SEQ ID NO: 6), LQVVFLR (SEQ ID NO: 7), LQVVWLH (SEQ ID NO: 8), LQVVWLK (SEQ ID NO: 9), LQVVWLR (SEQ ID NO: 10), LNVVYLH (SEQ ID NO: 11), LNVVYLK (SEQ ID NO: 12), LNVVYLR (SEQ ID NO: 13), LNVVFLH (SEQ ID NO: 14), LNVVFLK (SEQ ID NO: 15), LNVVFLR (SEQ ID NO: 16), LNVVWLH (SEQ ID NO: 17), LNVVWLK (SEQ ID NO: 18), LNVVWLR (SEQ ID NO: 19), and combinations thereof. In some embodiments, the peptide comprises LQVVYLH (SEQ ID NO: 2). In some embodiments, the peptide consists of LQVVYLH (SEQ ID NO: 2). In some embodiments, the peptide consists of an amino acid sequence that is less than 50 amino acids in length, optionally between 7 and 10 amino acids in length. In some embodiments, the peptide is formulated as a pharmaceutically acceptable salt. In some embodiments, the salt is an acid salt. In some embodiments, the salt is a trifluoracetic acid salt, an acetate salt, a hydrochloride salt, or a combinations thereof. In some embodiments, the salt is a trifluoracetic acid salt. In some embodiments, the peptide is an inhibitor of TGF-ȕ1 signaling. In some embodiments, the bulking agent is selected from lactose (e.g., lactose monohydrate), sucrose, lactose, trehalose, mannitol, sorbitol, glucose, rafinose, glycine, histidine, polyethylene glycol, polyvinyl pyrollidone, bovine serum albumin, dextran, and combinations thereof. In some embodiments, the bulking agent is lactose monohydrate. Attorney Docket No.55002-0003WO1 In some embodiments, the lyophilized composition consists essentially of the peptide and the bulking agent. In some embodiments, the lyophilized composition consists of the peptide, the bulking agent, and 5% wt/wt or less residual water. In some embodiments, the lyophilized composition consists of the peptide, the bulking agent, and 2% wt/wt or less residual water. In some embodiments, the lyophilized composition consists of the peptide, the bulking agent, and 1% wt/wt or less residual water. In some embodiments, the lyophilized composition comprises from 1% to 10% wt/wt of the peptide. In some embodiments, the lyophilized composition comprises from 2% to 5% wt/wt of the peptide. In some embodiments, the lyophilized composition comprises from 3.8% to 3.9% wt/wt of the peptide. In some embodiments, the residual water content is 5% wt/wt or less. In some embodiments, the residual water content is 2% wt/wt or less. In some embodiments, the residual water content is 1% wt/wt or less. In some embodiments, the residual water content is measured by Karl Fischer Titration, Thermogravimetric Analysis, Near Infra-red Spectroscopy, or Frequency Modulated Spectroscopy. In some embodiments, the residual water content is measured by Karl Fisher Titration. Also provided herein are containers comprising any of the compositions described herein. In some embodiments, the container is a plastic container or a glass container. In some embodiments, the plastic container is a polystyrene container or a polypropylene container. In some embodiments, the container is translucent or clear. In some embodiments, the container is chemically resistant or chemically inert. In some embodiments, the container is a vial. In some embodiments, the vial is an injection vial. In some embodiments, the vial is a glass injection vial. In some embodiments, the glass injection vial comprises a hydrophobic inner coating. In some embodiments, the hydrophobic inner coating is a chemically uniform hydrophobic inner coating. In some embodiments, the hydrophobic inner coating is a Si-O-C-H coating. In some embodiments, the hydrophobic inner coating is about 40 nm thick. In some embodiments, the coating is bonded covalently to the glass substrate. In some embodiments, the glass injection vial does not comprise a hydrophobic inner coating. In some embodiments, the container further comprises a stopper. In some embodiments, the stopper comprises a barrier film. In some embodiments, the barrier film is chemically inert. In some embodiments, the barrier film is a fluoropolymer film. In some embodiments, the fluoropolymer film is a Attorney Docket No.55002-0003WO1 poly(ethylene tetrafluoroethylene) (ETFE) fluoropolymer film. In some embodiments, the stopper does not comprise a barrier film. In some embodiments, the container has a volume capacity of from 2 ml to 100 ml. In some embodiments, the container is a 6 ml injection vial. In some embodiments, the container contains from 10 to 500 mg of the composition. In some embodiments, the container contains from 78 to 100 mg of the composition. In some embodiments, the container contains from 78 to 89 mg of the composition. In some embodiments, the container comprises at least 78 mg of the composition. In some embodiments, the lyophilized composition is stable for at least 1 month at 25°C ± 2°C. In some embodiments, the lyophilized composition is stable for at least 1 month at 25°C ± 2°C / 60% ± 5% Relative Humidity. In some embodiments, the lyophilized composition is stable for at least 1 month at 40°C ± 2°C. In some embodiments, the lyophilized composition is stable for at least 1 month at 5°C ± 3°C. In some embodiments, the lyophilized composition is stable for at least 2 months. In some embodiments, the lyophilized composition is stable for at least 3 months. In some embodiments, the lyophilized composition is stable for at least 6 months. In some embodiments, the composition is stable if the proportion of peptide in the composition does not decrease, or decreases by no more than 5%. In some embodiments, the composition is stable if the proportion of peptide in the composition does not decrease, or decreases by no more than 2%. In some embodiments, the composition is stable if the proportion of peptide in the composition does not decrease, or decreases by no more than 1%. In some embodiments, the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 0.5%. In some embodiments, the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 1%. In some embodiments, the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 2%. In some embodiments, the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 5%. In some embodiments, the proportion of peptide in the composition or the proportion of degradation product(s) in the composition is measured by liquid chromatography. In some embodiments, the liquid chromatography is ultra high-performance liquid chromatography (UPLC). Attorney Docket No.55002-0003WO1 In some embodiments, the composition is white to off white. In some embodiments, the composition is a lyophilized cake with no melt back. In some embodiments, the composition is a lyophilized cake with no collapse. Also provided herein are methods for producing a lyophilized composition comprising a peptide comprising or consisting of the amino acid sequence SGLPDLKLLQVVYLHSNNI (SEQ ID NO: 20) or fragment thereof (e.g., 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, or 18 consecutive amino acids of SEQ ID NO: 20), optionally with one or more conservative amino acid substitutions, or a pharmaceutically acceptable salt thereof, and a bulking agent, the method comprising: preparing or having prepared a solution comprising the peptide and the bulking agent; and lyophilizing the solution. In some embodiments, the peptide comprises or consists of the amino acid sequence L-X1-V-V-X2-L-X3, (SEQ ID NO: 1), where X1 is Q or N; X2 is Y, F, or W; X3 is H, K, or R; L is Leucine; Q is Glutamine, N is Asparagine, V is Valine, Y is Tyrosine, F is Phenylalanine, W is Tryptophan, H is Histidine, K is Lysine, and R is Arginine. In some embodiments, the peptide comprises or consists of an amino acid sequence selected from the group consisting of LQVVYLH (SEQ ID NO: 2), LQVVYLK (SEQ ID NO: 3), LQVVYLR (SEQ ID NO: 4), LQVVFLH (SEQ ID NO: 5), LQVVFLK (SEQ ID NO: 6), LQVVFLR (SEQ ID NO: 7), LQVVWLH (SEQ ID NO: 8), LQVVWLK (SEQ ID NO: 9), LQVVWLR (SEQ ID NO: 10), LNVVYLH (SEQ ID NO: 11), LNVVYLK (SEQ ID NO: 12), LNVVYLR (SEQ ID NO: 13), LNVVFLH (SEQ ID NO: 14), LNVVFLK (SEQ ID NO: 15), LNVVFLR (SEQ ID NO: 16), LNVVWLH (SEQ ID NO: 17), LNVVWLK (SEQ ID NO: 18), LNVVWLR (SEQ ID NO: 19), and combinations thereof. In some embodiments, the peptide comprises LQVVYLH (SEQ ID NO: 2). In some embodiments, the peptide consists of LQVVYLH (SEQ ID NO: 2). In some embodiments, the peptide consists of an amino acid sequence that is less than 50 amino acids in length, optionally between 7 and 10 amino acids in length. In some embodiments, the peptide is formulated as a pharmaceutically acceptable salt. In some embodiments, the salt is an acid salt. In some embodiments, the salt is a trifluoracetic acid salt, an acetate salt, a hydrochloride salt, or a combinations thereof. In some embodiments, the salt is a trifluoracetic acid salt. In some embodiments, the peptide is an inhibitor of TGF-ȕ1 signaling. Attorney Docket No.55002-0003WO1 In some embodiments, the bulking agent is selected from lactose (e.g., lactose monohydrate), sucrose, lactose, trehalose, mannitol, sorbitol, glucose, rafinose, glycine, histidine, polyethylene glycol, polyvinyl pyrollidone, bovine serum albumin, dextran, and combinations thereof. In some embodiments, the bulking agent is lactose monohydrate. In some embodiments, preparing or having prepared a solution comprising the peptide and the bulking agent comprises: preparing the peptide or having the peptide prepared; preparing or having prepared a solution comprising the bulking agent; and mixing the peptide and the solution comprising the bulking agent. In some embodiments, preparing the peptide or having the peptide prepared comprises synthesizing the peptide or having the peptide synthesized. In some embodiments, the peptide is lyophilized. In some embodiments, preparing or having prepared a solution comprising the bulking agent comprises: mixing the bulking agent with water or an aqueous solution. In some embodiments, preparing or having prepared a solution comprising the bulking agent comprises: mixing the bulking agent with water. In some embodiments, the method further comprises filtering the solution comprising the bulking agent. In some embodiments, the solution comprising the bulking agent comprises from 4 to 6% w/w of the bulking agent. In some embodiments, the solution comprising the bulking agent comprises from 4.5 to 5.5% w/w of the bulking agent. In some embodiments, the solution comprising the bulking agent comprises 5% w/w of the bulking agent or about 5% w/w of the bulking agent. In some embodiments, the solution comprising the peptide and the bulking agent comprises from 1.5 to 2.5 mg/ml of the peptide. In some embodiments, the solution comprising the peptide and the bulking agent comprises from 1.9 to 2.1 mg/ml of the peptide. In some embodiments, the pH of the solution comprising the peptide and the bulking agent is, or is adjusted to, 2–5. In some embodiments, the pH of the solution comprising the peptide and the bulking agent is, or is adjusted to, 2.5– 4. In some embodiments, the pH of the solution comprising the peptide and the bulking agent is, or is adjusted to, 3 or about 3. In some embodiments, mixing the peptide and the solution comprising the bulking agent comprises agitation for 30 minutes or less. In some embodiments, mixing the peptide and the solution comprising the bulking agent comprises agitation at 5 ± 3°C. In some embodiments, Attorney Docket No.55002-0003WO1 the method further comprises filtering the solution comprising the peptide and the bulking agent. In some embodiments, the method further comprises dispensing all or a portion of the solution comprising the peptide and the bulking agent into one or more container(s). In some embodiments, the container is a plastic container or a glass container. In some embodiments, the plastic container is a polystyrene container or a polypropylene container. In some embodiments, the container is translucent or clear. In some embodiments, the container is chemically resistant or chemically inert. In some embodiments, the container is a vial. In some embodiments, the vial is an injection vial. In some embodiments, the vial is a glass injection vial. In some embodiments, the glass injection vial comprises a hydrophobic inner coating. In some embodiments, the hydrophobic inner coating is a chemically uniform hydrophobic inner coating. In some embodiments, the hydrophobic inner coating is a Si-O-C-H coating. In some embodiments, the hydrophobic inner coating is about 40 nm thick. In some embodiments, the coating is bonded covalently to the glass substrate. In some embodiments, the glass injection vial does not comprise a hydrophobic inner coating. In some embodiments, the container has a volume of from 2 ml to 100 ml. In some embodiments, the container is a 6 ml injection vial. In some embodiments, dispensing all or a portion of the solution comprising the peptide and the bulking agent into a container comprises dispensing from 1.0 to 2.0 ml of the solution into the container. In some embodiments, dispensing all or a portion of the solution comprising the peptide and the bulking agent into a container comprises dispensing 1.7 ml or about 1.7 ml into the container. In some embodiments, dispensing all or a portion of the solution comprising the peptide and the bulking agent into a container comprises dispensing a volume of the solution comprising from 2.5 mg to 3.5 mg of the peptide into the container. In some embodiments, dispensing all or a portion of the solution comprising the peptide and the bulking agent into a container comprises dispensing a volume of the solution comprising 3.0 mg or about 3.0 mg of the peptide into the container. In some embodiments, the solution is dispensed into more than one container, optionally 100 or more containers, 500 or more, 1,000 or more, 5,000 or more, or 10,000 or more containers. In some embodiments, the solution is dispensed at a rate of from 10 to 100 containers per minute. In some embodiments, the solution is dispensed at a rate of at least 10 containers per minute, optionally at least 20, 30, or 40 containers per minute. Attorney Docket No.55002-0003WO1 In some embodiments, the method further comprises partially stoppering the filled container with a stopper. In some embodiments, the stopper comprises a barrier film. In some embodiments, the barrier film is chemically inert. In some embodiments, the barrier film is a fluoropolymer film. In some embodiments, the fluoropolymer film is a poly(ethylene tetrafluoroethylene) (ETFE) fluoropolymer film. In some embodiments, the stopper does not comprise a barrier film. In some embodiments, lyophilizing the solution comprises, in sequence: 1) a freezing stage; 2) a primary drying stage; and 3) a secondary drying stage. In some embodiments, the freezing stage comprises, in sequence: 1) a loading step; 2) a first freezing step; 3) an annealing step; and 4) a second freezing step. In some embodiments, the loading step comprises placing containers comprising the solution into a lyophilizer chamber, optionally at 5°C or about 5°C, optionally under atmospheric pressure. In some embodiments, the first freezing step comprises decreasing the temperature of the chamber to -50°C or to about -50°C under atmospheric pressure over the course of a ramp period, and holding the chamber at that temperature for a soak period, optionally wherein the ramp period is 55 minutes or about 55 minutes, and optionally wherein the soak period is 150 minutes or about 150 minutes. In some embodiments, the annealing step comprises increasing the temperature of the chamber to -10°C or about -10°C under atmospheric pressure over the course of a ramp period, and holding the chamber at that temperature for a soak period, optionally wherein the ramp period is 40 minutes or about 40 minutes, and optionally wherein the soak period is 150 minutes or about 150 minutes. In some embodiments, the first freezing step comprises decreasing the temperature of the chamber to -50°C or to about -50°C under atmospheric pressure over the course of a ramp period, and holding the chamber at that temperature for a soak period, optionally wherein the ramp period is 40 minutes or about 40 minutes, and optionally wherein the soak period is 120 minutes or about 120 minutes. In some embodiments, the primary drying stage comprises, in sequence: 1) decreasing the pressure of the chamber to 75 mTorr or about 75 mTorr while holding the temperature steady at -50°C or to about -50°C, and holding the chamber at that pressure and temperature for a soak period, optionally wherein the soak period is 60 minutes or about 60 minutes; and 2) increasing the temperature of the chamber to - 15°C or about -15°C and holding the pressure of the chamber steady at 75 mTorr or Attorney Docket No.55002-0003WO1 about 75 mTorr over the course of a ramp period, and holding the chamber at that temperature and pressure for a soak period, optionally wherein the ramp period is 35 minutes or about 35 minutes, and optionally wherein the soak period is 2184 minutes or about 2184 minutes. In some embodiments, the secondary drying stage comprises raising the temperature of the chamber to 5°C or about 5°C and holding the pressure of the chamber steady at 75 mTorr or about 75 mTorr over the course of a ramp period, and holding the chamber at that temperature and pressure for a soak period, optionally wherein the ramp period is 180 minutes or about 180 minutes, and optionally wherein the soak period is 600 minutes or about 600 minutes. In some embodiments, the method further comprises back-filling the containers with an inert gas and fully stoppering with a stopper. In some embodiments, the inert gas is nitrogen. In some embodiments, back-filling the containers with an inert gas and fully stoppering with a stopper is carried out at 5°C or about 5°C, optionally at 600,000 mTorr or about 600,000 mTorr. In some embodiments, the stopper comprises a barrier film. In some embodiments, the barrier film is chemically inert. In some embodiments, the barrier film is a fluoropolymer film. In some embodiments, the fluoropolymer film is a poly(ethylene tetrafluoroethylene) (ETFE) fluoropolymer film. In some embodiments, the container and stopper comprising the solution comprising the peptide and the bulking agent are the same as the container and stopper comprising the lyophilized solution comprising the peptide and the bulking agent. In some embodiments, the method further comprises sealing the container. In some embodiments, the container is sealed with a flip-off seal. In some embodiments, the method further comprises one or more of: inspecting, packaging, shipping, storing, or labeling the container(s). Also provided herein are lyophilized compositions produced according to any of the methods described herein. In some embodiments, the lyophilized composition is stable for at least 1 month at 25°C ± 2°C. In some embodiments, the lyophilized composition is stable for at least 1 month at 25°C ± 2°C / 60% ± 5% Relative Humidity. In some embodiments, the lyophilized composition is stable for at least 1 month at 40°C ± 2°C. In some embodiments, the lyophilized composition is stable for at least 2 months. In some embodiments, the lyophilized composition is stable for Attorney Docket No.55002-0003WO1 at least 3 months. In some embodiments, the lyophilized composition is stable for at least 6 months. In some embodiments, the lyophilized composition is stable if the proportion of peptide in the composition does not decrease, or decreases by no more than 5%. In some embodiments, the composition is stable if the proportion of peptide in the composition does not decrease, or decreases by no more than 2%. In some embodiments, the composition is stable if the proportion of peptide in the composition does not decrease, or decreases by no more than 1%. In some embodiments, the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 0.5%. In some embodiments, the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 1%. In some embodiments, the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 2%. In some embodiments, the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 5%. In some embodiments, the proportion of peptide in the composition or the proportion of degradation product(s) in the composition is measured by liquid chromatography. In some embodiments, the liquid chromatography is ultra high-performance liquid chromatography (UPLC). In some embodiments, the composition is white to off white. In some embodiments, the composition is a lyophilized cake with no melt back. In some embodiments, the composition is a lyophilized cake with no collapse. Also provided herein is the use of a peptide a peptide comprising or consisting of the amino acid sequence SGLPDLKLLQVVYLHSNNI (SEQ ID NO: 20) or fragment thereof (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, or 18 consecutive amino acids of SEQ ID NO: 20), optionally with one or more conservative amino acid substitutions, or pharmaceutically acceptable salt thereof; and/or a bulking agent in the production of a lyophilized composition comprising the peptide and the bulking agent. Also provided herein are methods for producing an injectable composition, the method comprising: reconstituting a lyophilized composition described herein, or the lyophilized composition within a container described herein in a pharmaceutically acceptable carrier, thereby producing an injectable composition. In some embodiments, the pharmaceutically acceptable carrier is water or saline. In some embodiments, the pharmaceutically acceptable carrier is saline. In some Attorney Docket No.55002-0003WO1 embodiments, the pharmaceutically acceptable carrier is 0.9% saline. In some embodiments, the injectable composition comprises 2.0 mg/ml of the peptide or about 2.0 mg/ml. In some embodiments, the injectable composition comprises 50 mg/ml of the bulking agent or about 50 mg/ml of the bulking agent. In some embodiments, the injectable composition has a pH of from 2 to 4.5. In some embodiments, the pH of the injectable composition is from 2.5 to 4. In some embodiments, the pH of the injectable composition is 3 or about 3. Also provided herein are injectable compositions produced according the methods described herein Also provided herein is the use of a lyophilized composition described herein, or the lyophilized composition within a container described herein; and/or a pharmaceutically acceptable carrier in the production of an injectable composition. Also provided herein are kits comprising: a container comprising a lyophilized composition described herein, and a syringe. In some embodiments, the kit further comprises a reconstitution needle, optionally a 21 G x 1.5 in needle. In some embodiments, the kit further comprises an injection needle, optionally a 22 G x 7 in quincke type point needle. In some embodiments, the syringe is a 1, 2, 3, 4, or 5 cc syringe. In some embodiments, the syringe is a 3 cc syringe. In some embodiments, the kit further comprises instructions for administration. Also provided herein are methods comprising: administering an injectable composition described herein to a patient. Also provided herein are methods of inhibiting TGF-ȕ1 in cell(s) of a patient, the method comprising: administering an injectable composition described herein to the patient. Also provided herein are methods of treating a patient with a disease or disorder associated with overexpression of TGF-ȕ1, the method comprising: administering an injectable composition described herein to the patient. In some embodiments, the composition is administered by injection, optionally intradiscal injection. Throughout this application, various embodiments may be presented in a range format. It should be understood that the description in range format is merely for convenience and brevity and should not be construed as an inflexible limitation on the scope of the disclosure. Accordingly, the description of a range should be considered to have specifically disclosed all the possible subranges as well as individual numerical values within that range. For example, description of a range Attorney Docket No.55002-0003WO1 such as from 1 to 6 should be considered to have specifically disclosed subranges such as from 1 to 3, from 1 to 4, from 1 to 5, from 2 to 4, from 2 to 6, from 3 to 6 etc., as well as individual numbers within that range, for example, 1, 2, 3, 4, 5, and 6. This applies regardless of the breadth of the range. As used in the specification and claims, the singular forms “a,” “an” and “the” include plural references unless the context clearly dictates otherwise. For example, the term “a sample” includes a plurality of samples, including mixtures thereof. The terms “determining,” “measuring,” “evaluating,” “assessing,” “assaying,” and “analyzing” are often used interchangeably herein to refer to forms of measurement. The terms include determining if an element is present or not (for example, detection). These terms can include quantitative, qualitative or quantitative and qualitative determinations. Assessing can be relative or absolute. “Detecting the presence of” can include determining the amount of something present in addition to determining whether it is present or absent depending on the context. As used herein, the term “about” a number refers to that number plus or minus 10% of that number. The term “about” a range refers to that range minus 10% of its lowest value and plus 10% of its greatest value. Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Methods and materials are described herein for use in the present invention; other, suitable methods and materials known in the art can also be used. The materials, methods, and examples are illustrative only and not intended to be limiting. All publications, patent applications, patents, sequences, database entries, and other references mentioned herein are incorporated by reference in their entirety. In case of conflict, the present specification, including definitions, will control. Other features and advantages of the invention will be apparent from the following detailed description and figures, and from the claims. DETAILED DESCRIPTION Described herein are, among other things, new peptide formulations, and methods of manufacturing the same. Attorney Docket No.55002-0003WO1 LYOPHILIZED DRUG PRODUCT FORMULATIONS The lyophilized drug product formulations described herein comprise peptide(s) and/or pharmaceutically acceptable salt(s) thereof (e.g., as described herein) and bulking agent(s) (e.g., as described herein). Peptides The compositions and methods described herein comprise peptide(s) and/or pharmaceutically acceptable salts thereof. In some cases, the peptide comprises or consists of the amino acid sequence SGLPDLKLLQVVYLHSNNI (SEQ ID NO: 20) or fragment thereof (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, or 18 consecutive amino acids of SEQ ID NO: 20), optionally with one or more conservative amino acid substitutions. In some cases, the peptide comprises or consists of the amino acid sequence LQVVYLH (SEQ ID NO: 2) with one or more conservative amino acid substitutions. The terms “conservative sequence modifications” or “conservative substitutions” as used herein may refer to amino acid modifications to a peptide of the disclosure that does not significantly affect or alter the functional characteristic(s) of the peptide, e.g., the ability to as described herein, e.g., inhibition of TGF-ȕ1 signaling. “Conservative substitution” as used herein refers to a substitution in which one amino acid residue is replaced with another amino acid residue having a similar side chain. Families of amino acid residues having similar side chains have been generally defined in the art, including basic side chains (e.g., lysine, arginine, histidine), acidic side chains (e.g., aspartic acid, glutamic acid), uncharged polar side chains (e.g., glycine, asparagine, glutamine, serine, threonine, tyrosine, cysteine), nonpolar side chains (e.g., alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, tryptophan), beta-branched side chains (e.g., threonine, valine, isoleucine) and aromatic side chains (e.g., tyrosine, phenylalanine, tryptophan, histidine). For example, substitution of a phenylalanine for a tyrosine is considered to be a conservative substitution. Methods of identifying amino acid conservative substitutions that do not eliminate binding are well-known in the art. In some cases, the peptide comprises or consists of the amino acid sequence L- X1-V-V-X2-L-X3, (SEQ ID NO: 1) where X1 is an amidic amino acid with a polar uncharged side chain (i.e., Q or N); X₂ is an aromatic amino acid with a hydrophobic side chain (i.e., Y, F, or W); X3 is an amino acid with a positively charged side chain Attorney Docket No.55002-0003WO1 (i.e., H, K, or R); L is Leucine; Q is Glutamine, N is Asparagine, V is Valine, Y is Tyrosine, F is Phenylalanine, W is Tryptophan, H is Histidine, K is Lysine, and R is Arginine. In some cases, the peptide comprises or consists of an amino acid sequence selected from the group consisting of LQVVYLH (SEQ ID NO: 2), LQVVYLK (SEQ ID NO: 3), LQVVYLR (SEQ ID NO: 4), LQVVFLH (SEQ ID NO: 5), LQVVFLK (SEQ ID NO: 6), LQVVFLR (SEQ ID NO: 7), LQVVWLH (SEQ ID NO: 8), LQVVWLK (SEQ ID NO: 9), LQVVWLR (SEQ ID NO: 10), LNVVYLH (SEQ ID NO: 11), LNVVYLK (SEQ ID NO: 12), LNVVYLR (SEQ ID NO: 13), LNVVFLH (SEQ ID NO: 14), LNVVFLK (SEQ ID NO: 15), LNVVFLR (SEQ ID NO: 16), LNVVWLH (SEQ ID NO: 17), LNVVWLK (SEQ ID NO: 18), LNVVWLR (SEQ ID NO: 19), and combinations thereof. In some cases, the peptide consists of an amino acid sequence that is between 7 and 50 amino acids in length, e.g., 7 and 45, 7 and 40, 7 and 35, 7 and 30, 7 and 25, 7 and 20, 7 and 15, 7 and 14, 7 and 13, 7 and 12, 7 and 11, 7 and 10, 7 and 9, 7 and 8, 8 and 50, 8 and 45, 8 and 40, 8 and 35, 8 and 30, 8 and 25, 8 and 20, 8 and 15, 8 and 14, 8 and 13, 8 and 12, 8 and 11, 8 and 10, 8 and 9, 9 and 50, 9 and 45, 9 and 40, 9 and 35, 9 and 30, 9 and 25, 9 and 20, 9 and 15, 9 and 14, 9 and 13, 9 and 12, 9 and 11, 9 and 10, 10 and 50, 10 and 45, 10 and 40, 10 and 35, 10 and 30, 10 and 25, 10 and 20, 10 and 15, 10 and 14, 10 and 13, 10 and 12, 10 and 11, 11 and 50, 11 and 45, 11 and 40, 11 and 35, 11 and 30, 11 and 25, 11 and 20, 11 and 15, 11 and 14, 11 and 13, 11 and 12, 12 and 50, 12 and 45, 12 and 40, 12 and 35, 12 and 30, 12 and 25, 12 and 20, 12 and 15, 12 and 14, 12 and 13, 13 and 50, 13 and 45, 13 and 40, 13 and 35, 13 and 30, 13 and 25, 13 and 20, 13 and 15, 13 and 14, 14 and 50, 14 and 45, 14 and 40, 14 and 35, 14 and 30, 14 and 25, 14 and 20, 14 and 15, 15 and 50, 15 and 45, 15 and 40, 15 and 35, 15 and 30, 15 and 25, 15 and 20, 20 and 50, 20 and 45, 20 and 40, 20 and 35, 20 and 30, 20 and 25, 25 and 50, 25 and 45, 25 and 40, 25 and 35, 25 and 30, 30 and 50, 30 and 45, 30 and 40, 30 and 35, 35 and 50, 35 and 45, 35 and 40, 40 and 50, 40 and 45, or 45 and 50 amino acids in length. In some cases, the peptide consists of an amino acid sequence that is 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, or 50 amino acids long. In some cases, the peptide is less than 50 amino acids long. Attorney Docket No.55002-0003WO1 Examples of pharmaceutically acceptable salts include hydrochloride, sulfate, phosphate, lactate, maleate, fumarate, oxalate, methanesulfonate, p-toluenesulfonate, and the like. In some cases, the salt is an acid addition salt. In some cases, the salt is a base addition salt. In some cases, the peptide(s) are prepared as a trifluoracetic acid (TFA) salt. In some cases, the peptide(s) are prepared as an acetate salt. In some cases, the peptide(s) are prepared as a hydrochloride (HCl) salt. In some cases, the peptides inhibit or promote cellular processes, e.g., as described herein, e.g., a cellular signaling process, e.g., TGF-ȕ1 signaling. In some cases, the inhibition or promotion is direct (e.g., inhibition or promotion of TGF-ȕ1 signaling by binding to the TGF-ȕ receptor). In some cases, the inhibition or promotion is indirect (e.g., by altering a regulatory cascade). In some cases, the inhibition or promotion is in comparison to a control. In some cases, the control is a non-diseased cell or tissue. In some cases, the control is a diseased cell or tissue, prior to the administration of the peptide. TGF-ȕ is known as a highly pleiotropic cytokine that plays an important role in apoptosis control, angiogenesis, wound healing, immune regulation, and tumor biology. TGF-ȕ exists in three isoforms: TGF-ȕ1, TGF-ȕ2, and TGF-ȕ3. All three TGF-ȕs use the same receptor. The TGF-ȕ receptor has three components: type I (RI or ALK5), type II (RII), and type III (RIII or betaglycan). TGF-ȕ (all isoforms) binds RIII and recruits RII, which then phosphorylates RI to form a heterotetrameric serine/threonine kinase complex. In turn, RI phosphorylates Smad2 and Smad3 (receptor-associated Smads (R-Smads)), and the latter form a heteromeric complex with Smad4, which translocates to the nucleus, binds to DNA and regulates transcription (Prud'homme, Lab Invest 87:1077-1091, 2007). In some cases, the peptide binds TGF-ȕ1. In some cases, the peptide inhibits TGF-ȕ1 signaling. In some cases, the peptide partially inhibits TGF-ȕ1 signaling. In some cases, the peptide completely inhibits TGF-ȕ1 signaling. In some cases, the peptide inhibits TGF-ȕ1 signaling by binding to the TGF-ȕ receptor and inhibiting binding of TGF-ȕ1 to the receptor. In some cases, inhibition of TGF-ȕ1 signaling results in failure of Smad2 and Smad3 to undergo phosphorylation, and, therefore, failing to form a complex with Smad4, which, in turn, results in a failure of the complex to translocate to the nucleus and regulate transcription. Attorney Docket No.55002-0003WO1 In some cases, the peptide inhibits the catabolic effect of overexpression of TGF-ȕ1. In some cases, the peptide inhibits the ALK1-Smad1/5/8 pathway. In some cases, the peptide promotes (increases) synthesis of ECM components in a cell. In some cases, the ECM components comprise Aggrecan and/or Type II Collagen. Synthesis and Modifications The chemical synthesis of peptides is a well-developed field. Methods for peptide synthesis include, for example, solid-phase peptide synthesis such as Fmoc- SPPS and Boc-SPPS The peptide(s) of the present application can be prepared as described, for example, in US Patent No.8,691,749, which is hereby incorporated by reference in its entirety. In some cases, the peptides are modified, e.g., for stabilization. A number of peptide modifications, e.g., for stabilization of the peptide while maintaining biological activity, are known in the art and contemplated herein. See, e.g., Wang et al., “Therapeutic Peptides: Current Applications and Future Directions,” Signal Transduction and Targeted Therapy 7:48 (2002). In some cases, the peptide is N- and/or C- terminal protected, e.g., to reduce proteolytic degradation and/or improve bioavailability. In some cases, an N- terminal Pro, Glu, Ser, or Thr, is replaced with an N-terminal Met, Ser, Ala, Thr, Val, or Gly, e.g., to improve resistance to proteolysis and degradation in plasma. In some cases, the peptide is C-terminal amidated. In some cases, the peptide is N-terminal acetylated. In some cases, the peptide is backbone modified. In some cases, backbone modification comprises substitution of natural amino acid(s) for non-natural amino acid(s). In some cases, the backbone modification includes one or more of: the substitution of L-amino acids by D-amino acids, insertions of methyl-amino acids, and the incorporation of ȕ-amino acids. In some cases, the peptide is backbone modified at a proteolytic site, e.g., a proteolytic site identified by stability studies and/or metabolite determination. In some cases, the peptide is side chain modified. In some cases, side chain modification comprises replacing a natural amino acid with an analogue during peptide synthesis. In some cases, the analogue is selected from homoarginine, benzyloxy-tyrosine, ȕ-phenylalanine, and combinations thereof. Attorney Docket No.55002-0003WO1 In some cases, the peptide is PEGylated. In some cases, the modified peptide retains the activity of the unmodified peptide, e.g., an activity described herein, e.g., inhibition of TGF-ȕ1. Bulking Agents The lyophilized drug product formulations described herein comprise bulking agent(s) in addition to the peptides. In some cases the bulking agent comprises or consists of lactose, e.g., lactose monohydrate ((2R,3R,4S,5R,6S)-2-(hydroxymethyl)-6-[(2R,3S,4R,5R,6S)-4,5,6- trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxane-3,4,5-triol;hydrate). Examples of grades/types of lactose monohydrate include without limitation DCL 11, Flowlac® 100, Inhalac® 230, Lactohale® 300, Lactopress® SD 250 (spray- dried lactose), Respitose® SV003 and Sorbolac® 400. The formulations described herein can contain a single lactose grade or a combination of different lactose grades. Other bulking agents include, without limitation, sucrose, lactose, trehalose, mannitol, sorbitol, glucose, rafinose, glycine, histidine, polyethylene glycol, polyvinyl pyrollidone, bovine serum albumin, dextran, and combinations thereof. Additional Excipients In some cases, the formulations described herein comprise excipient(s) including, but not limited to tonicity modifier(s), buffering agent(s), solubilizing agent(s), complexing / dispersing agent(s), cryoprotectant(s), lyoprotectant(s), surfactant(s), antioxidant(s), preservative(s), chelating agent(s), and combinations thereof. Tonicity modifiers include, without limitation, dextrose, dextran, ficoll, gelatin, hydroxyethyl, starch, glycerol, sodium chloride, glycerin, mannitol, and combinations thereof. Buffering agents include, without limitation, citrate, phosphate, Tris (e.g., Tris base-65, Tris acetate, or Tris HCl-65), succinate, tartrate, acetate, and combinations thereof. Solubilizing agents include, without limitation, Polyoxyethylenes (Tween) and Lecithin. In some cases, the solubilizing agent is a co-solvent, including, for example, propylene glycol, glycerin, ethanol, polyethylene glycol, sorbitol, dimethylacetamide, and combinations thereof. Attorney Docket No.55002-0003WO1 METHODS OF MANUFACTURING Provided herein are methods of manufacturing the lyophilized compositions described herein. Also provided herein are methods of packaging the compositions, and methods of preparing an injectate from the compositions. Preparation of Lyophilized Drug Product In some cases, the method of manufacturing the lyophilized composition comprises preparing or having prepared a solution comprising, consisting of, or consisting essentially of, the peptide (e.g., as described herein) and the bulking agent (e.g., as described herein). In some cases, preparing or having prepared the solution comprises, consists of, or consists essentially of, preparing the peptide or having the peptide prepared (e.g., a peptide described herein, e.g., SEQ ID NO: 2); preparing a solution comprising the bulking agent or having prepared a solution comprising the bulking agent; and mixing the peptide and the solution comprising the bulking agent. In some cases, preparing the peptide or having the peptide prepared comprises synthesizing the peptide or having the peptide synthesized. In some cases, the peptide is lyophilized. In some cases, preparing or having prepared a solution comprising the bulking agent comprises mixing the bulking agent with water or an aqueous solution. In some cases, the method further comprises filtering the solution comprising the bulking agent. In some cases, the solution comprising the bulking agent comprises from 1 to 10% w/w of the bulking agent (e.g., lactose monohydrate), e.g., from 1 to 9, 1 to 8, 1 to 7, 1 to 6, 1 to 5, 1 to 4, 1 to 3, 1 to 2, 2 to 10, 2 to 9, 2 to 8, 2 to 7, 2 to 6, 2 to 5, 2 to 4, 2 to 3, 3 to 10, 3 to 9, 3 to 8, 3 to 7, 3 to 6, 3 to 5, 3 to 4, 4 to 10, 4 to 9, 4 to 8, 4 to 7, 4 to 6, 4 to 5, 5 to 10, 5 to 9, 5 to 8, 5 to 7, 5 to 6, 6 to 10, 6 to 9, 6 to 8, 6 to 7, 7 to 10, 7 to 9, 7 to 8, 8 to 10, 8 to 9, or 9 to 10% w/w. In some cases, the solution comprising the peptide and the bulking agent comprises from 0.1 to 10 mg/ml of the peptide or pharmaceutically acceptable salt thereof, e.g., from 0.1 to 9, 0.1 to 8, 0.1 to 7, 0.1 to 6, 0.1 to 5, 0.1 to 4, 0.1 to 3, 0.1 to 2, 0.1 to 1, 1 to 10, 1 to 9, 1 to 8, 1 to 7, 1 to 6, 1 to 5, 1 to 4, 1 to 3, 1 to 2, 2 to 10, 2 to 9, 2 to 8, 2 to 7, 2 to 6, 2 to 5, 2 to 4, 2 to 3, 3 to 10, 3 to 9, 3 to 8, 3 to 7, 3 to 6, 3 to 5, 3 to 4, 4 to 10, 4 to 9, 4 to 8, 4 to 7, 4 to 6, 4 to 5, 5 to 10, 5 to 9, 5 to 8, 5 to 7, 5 to 6, 6 to 10, 6 to 9, 6 to 8, 6 to 7, 7 to 10, 7 to 9, 7 to 8, 8 to 10, 8 to 9, or 9 to 10 Attorney Docket No.55002-0003WO1 mg/ml. In some cases, the solution comprises from 1.5 to 2.5 mg/ml of the peptide. In some cases, the solution comprises from 1.9 to 2.1 mg/ml of the peptide. In some cases, the pH of the solution comprising the peptide and the bulking agent is, or is adjusted to, 2 to 5, e.g., 2 to 4.5, 2 to 4, 2 to 3.5, 2 to 3, 2 to 2.5, 2.5 to 5, 2.5 to 4.5, 2.5 to 4, 2.5 to 3.5, 2.5 to 3, 3 to 5, 3 to 4.5, 3 to 4, 3 to 3.5, 3.5 to 5, 3.5 to 4.5, 3.5 to 4, 4 to 5, 4 to 4.5, or 4.5 to 5, any value within the range, or about any value within the range. In some cases, the pH of the solution comprising the peptide and the bulking agent is, or is adjusted to, 2 or about 2, 2.5 or about 2.5, 3 or about 3, 3.5 or about 3.5, 4 or about 4, 4.5 or about 4.5, or 5 or about 5. In some cases, the method comprises mixing the peptide and the solution comprising the bulking agent. In some cases, mixing comprises agitating for 24 hours or less, e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, or 23 hours or less. In some cases, mixing comprises agitating for 30 minutes or less. In some cases, mixing is carried out at room temperature. In some cases, mixing is carried out under refrigeration. In some cases, mixing is carried out 5 ± 3°C. In some cases, the method further comprises filtering the solution comprising the peptide and the bulking agent. In some cases, the method further comprises dispensing all or a portion of the solution comprising the peptide and the bulking agent into one or more container(s). In some cases, the container is a plastic container or a glass container. In some cases, the plastic container is a polystyrene container or a polypropylene container. In some cases, the container is translucent. In some cases, the container is clear. In some cases, the container is chemically resistant or chemically inert. In some cases, the container is a vial, e.g., an injection vial. In some cases, the container is a glass injection vial. In some cases, the glass injection vial comprises an inner coating, e.g., a hydrophobic inner coating. In some cases, the inner coating is a chemically uniform inner coating. In some cases, the inner coating is a Si-O-C-H coating. In some cases, the inner coating is or is about 40 nm thick. In some cases, the coating is bonded covalently to the glass substrate. In some cases, the glass injection vial does not comprise an inner coating. In some cases, the container has a volume of from 2 ml to 100 ml, e.g, 2 to 90, 2 to 80, 2 to 70, 2 to 60, 2 to 50, 2 to 40, 2 to 30, 2 to 20, 2 to 10, 2 to 5, 5 to 100, 5 to 90, 5 to 80, 5 to 70, 5 to 60, 5 to 50, 5 to 40, 5 to 30, 5 to 20, 5 to 10, 10 to 100, 10 to 90, 10 to 80, 10 to 70, 10 to 60, 10 to 50, 10 to 40, 10 to 30, 10 to 20, 20 to 100, 20 to Attorney Docket No.55002-0003WO1 90, 20 to 80, 20 to 70, 20 to 60, 20 to 50, 20 to 40, 20 to 30, 30 to 100, 30 to 90, 30 to 80, 30 to 70, 30 to 60, 30 to 50, 30 to 40, 40 to 100, 40 to 90, 40 to 80, 40 to 70, 40 to 60, 40 to 50, 50 to 100, 50 to 90, 50 to 80, 50 to 70, 50 to 60, 60 to 100, 60 to 90, 60 to 80, 60 to 70, 70 to 100, 70 to 90, 70 to 80, 80 to 100, 80 to 90, or 90 to 100 ml. In some cases, the container has a volume of 2 ml or about 2 ml, 3 ml or about 3 ml, 4 ml or about 4 ml, 5 ml or about 5 ml, 6 ml or about 6 ml, 7 ml or about 7 ml, 8 ml or about 8 ml, 9 ml or about 9 ml, 10 ml or about 10 ml, 11 ml or about 11 ml, 12 ml or about 12 ml. In some cases, the container is a 6 ml injection vial, e.g., glass injection vial (e.g., as described herein). In some cases, dispensing all or a portion of the solution into a container comprises dispensing from 1 to 100 ml, e.g., 1 to 90, 1 to 80, 1 to 70, 1 to 60, 1 to 50, 1 to 40, 1 to 30, 1 to 20, 1 to 10, 2 to 100, 2 to 90, 2 to 80, 2 to 70, 2 to 60, 2 to 50, 2 to 40, 2 to 30, 2 to 20, 2 to 10, 2 to 5, 5 to 100, 5 to 90, 5 to 80, 5 to 70, 5 to 60, 5 to 50, 5 to 40, 5 to 30, 5 to 20, 5 to 10, 10 to 100, 10 to 90, 10 to 80, 10 to 70, 10 to 60, 10 to 50, 10 to 40, 10 to 30, 10 to 20, 20 to 100, 20 to 90, 20 to 80, 20 to 70, 20 to 60, 20 to 50, 20 to 40, 20 to 30, 30 to 100, 30 to 90, 30 to 80, 30 to 70, 30 to 60, 30 to 50, 30 to 40, 40 to 100, 40 to 90, 40 to 80, 40 to 70, 40 to 60, 40 to 50, 50 to 100, 50 to 90, 50 to 80, 50 to 70, 50 to 60, 60 to 100, 60 to 90, 60 to 80, 60 to 70, 70 to 100, 70 to 90, 70 to 80, 80 to 100, 80 to 90, or 90 to 100 ml into the container. In some cases, dispensing all or a portion of the solution comprises dispensing from 1.0 to 2.0 ml of the solution into the container, e.g., 1.7 ml or about 1.7 ml. In some cases, dispensing all or a portion of the solution into a container comprises dispensing a volume of the solution comprising 1 to 10 mg of the peptide into the container, e.g., dispensing a volume of the solution comprising 1 to 9, 1 to 8, 1 to 7, 1 to 6, 1 to 5, 1 to 4, 1 to 3, 1 to 2, 2 to 10, 2 to 9, 2 to 8, 2 to 7, 2 to 6, 2 to 5, 2 to 4, 2 to 3, 3 to 10, 3 to 9, 3 to 8, 3 to 7, 3 to 6, 3 to 5, 3 to 4, 4 to 10, 4 to 9, 4 to 8, 4 to 7, 4 to 6, 4 to 5, 5 to 10, 5 to 9, 5 to 8, 5 to 7, 5 to 6, 6 to 10, 6 to 9, 6 to 8, 6 to 7, 7 to 10, 7 to 9, 7 to 8, 8 to 10, 8 to 9, or 9 to 10 mg of the peptide. In some cases, dispensing all or a portion of the solution into a container comprises dispensing a volume of the solution comprising from 1.7 to 1.8 mg of the peptide into the container, e.g., 1.729 or about 1.729 mg of the peptide. In some cases, the solution is dispensed into more than one container, e.g., 100 or more, 500 or more, 1,000 or more, 5,000 or more, or 10,000 or more containers. In some cases, the solution is dispensed at a rate of from 10 to 100 containers per Attorney Docket No.55002-0003WO1 minute. In some cases, the solution is dispensed at a rate of at least 10 containers per minute, e.g., at least 20, 30, or 40 containers per minute. In some cases, the method further comprises partially stoppering the filled container with a stopper. In some cases, the stopper comprises a barrier film. In some case, the film is chemically inert. In some cases, the film is a fluoropolymer film. In some cases, the fluoropolymer film is a poly(ethylene tetrafluoroethylene) (ETFE) fluoropolymer film. In some cases, the stopper does not comprise a barrier film. In some cases, the stopper is dried. In some cases, the stopper is autoclaved. Methods for lyophilization are well known in the art. See, e.g., Jennings, T.A. (1999). Lyophilization: Introduction and Basic Principles (1st ed.). CRC Press. https://doi.org/10.1201/b14424. In some cases, lyophilizing the solution comprises, in sequence: 1) a freezing stage; 2) a primary drying stage; and 3) a secondary drying stage. In some cases, the freezing stage comprises, in sequence: 1) a loading step; 2) a first freezing step; 3) an annealing step; and 4) a second freezing step. In some cases, the loading step comprises placing containers comprising the solution into a lyophilizer chamber, optionally at 5°C or about 5°C, optionally under atmospheric pressure. In some cases, the first freezing step comprises decreasing the temperature of the chamber to -50°C or to about -50°C under atmospheric pressure over the course of a ramp period, and holding the chamber at that temperature for a soak period, optionally wherein the ramp period is 55 minutes or about 55 minutes, and optionally wherein the soak period is 150 minutes or about 150 minutes. In some cases, the annealing step comprises increasing the temperature of the chamber to -10°C or about -10°C under atmospheric pressure over the course of a ramp period, and holding the chamber at that temperature for a soak period, optionally wherein the ramp period is 40 minutes or about 40 minutes, and optionally wherein the soak period is 150 minutes or about 150 minutes. In some cases, the first freezing step comprises decreasing the temperature of the chamber to -50°C or to about -50°C under atmospheric pressure over the course of a ramp period, and holding the chamber at that temperature for a soak period, optionally wherein the ramp period is 40 minutes or about 40 minutes, and optionally wherein the soak period is 120 minutes or about 120 minutes. Attorney Docket No.55002-0003WO1 In some cases, the primary drying stage comprises, in sequence: 1) decreasing the pressure of the chamber to 75 mTorr or about 75 mTorr while holding the temperature steady at -50°C or to about -50°C, and holding the chamber at that pressure and temperature for a soak period, optionally wherein the soak period is 60 minutes or about 60 minutes; and 2) increasing the temperature of the chamber to - 15°C or about -15°C and holding the pressure of the chamber steady at 75 mTorr or about 75 mTorr over the course of a ramp period, and holding the chamber at that temperature and pressure for a soak period, optionally wherein the ramp period is 35 minutes or about 35 minutes, and optionally wherein the soak period is 2184 minutes or about 2184 minutes. In some cases, the secondary drying stage comprises raising the temperature of the chamber to 5°C or about 5°C and holding the pressure of the chamber steady at 75 mTorr or about 75 mTorr over the course of a ramp period, and holding the chamber at that temperature and pressure for a soak period, optionally wherein the ramp period is 180 minutes or about 180 minutes, and optionally wherein the soak period is 600 minutes or about 600 minutes. In some cases, the method further comprises back-filling the containers with an inert gas and fully stoppering with a stopper. In some cases, the inert gas is nitrogen. In some cases, back-filling the containers with an inert gas and fully stoppering with a stopper is carried out at 5°C or about 5°C, optionally at 600,000 mTorr or about 600,000 mTorr. In some cases, the stopper comprises a barrier film. In some cases, the barrier film is chemically inert. In some cases, the barrier film is a fluoropolymer film. In some cases, the fluoropolymer film is a poly(ethylene tetrafluoroethylene) (ETFE) fluoropolymer film. In some cases, the stopper is dried. In some cases, the stopper is autoclaved. In some cases, the method comprises fully stoppering the container with the same stopper that was used to partially stopper it. In some cases, the method further comprises sealing the container. In some cases, the container is sealed with a flip-off seal. In some cases, the method further comprising one or more of: inspecting, packaging, shipping, storing, or labeling the container(s). Attorney Docket No.55002-0003WO1 LYOPHILIZED DRUG PRODUCT CHARACTERISTICS In some cases, the lyophilized drug product, e.g., manufactured as described herein, is characterized by one or more of: dose uniformity, stability, sterility, and visual appearance. In some cases, dose uniformity is measured by content uniformity. In some cases, dose uniformity is measured as weight uniformity. In some cases, a container comprising a lyophilized composition described herein comprises within 10%, e.g., within 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, or 1% of a target peptide content or weight. In some cases, when manufactured as described herein, at least 80%, e.g., at least 85%, 90% 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% of the filled vials comprise within 10%, e.g., within 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, or 1% of the target weight of the lyophilized composition. In some cases, at least 80%, e.g., at least 85%, 90% 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% of the filled vials comprise within 10%, e.g., within 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, or 1% of the target weight of the lyophilized composition. The formulations described herein were surprisingly found to be remarkably stable under a wide range of conditions, as shown, for example, in Example 4. Stability of drug substances is routinely done (e.g., as a part of the regulatory approval process) and methods for testing drug stability are well known in the art. When discussing stability, a stability of a certain amount of time is typically ascertained by comparing a starting value obtained at one time point to the value generated from the same test, on the same sample, at a later time. In some cases, stability is measured on a container level (e.g., single vial). In some cases, stability is measured on a batch level (e.g., across multiple vials of a single batch of lyophilized composition, manufactured, e.g., as described herein). In some cases, a composition is stable if the amount of peptide in the composition does not decrease, or if it decreases less than a certain amount, e.g., 10% or less, e.g., 9%, 8%, 7%, 6% 5%, 4%, 3%, 2%, or 1% or less. In some cases, a composition is stable if the amount of degradation product in the composition does not increase, or if it increases less than a certain amount, e.g., 10% or less e.g., 9%, 8%, 7%, 6% 5%, 4%, 3%, 2%, or 1% or less. In some cases, the lyophilized compositions described herein are stable at - 20°C for at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12 months. In some cases, the Attorney Docket No.55002-0003WO1 lyophilized compositions described herein are stable at 5°C for at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12 months. In some cases, the lyophilized compositions described herein are stable at 25°C (e.g., 25°C/60% RH ) for at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12 months. In some cases, the lyophilized compositions are stable at 40°C for at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11 or 12 months. In some cases, the visual appearance of the lyophilized composition is white or off-white. In some cases the lyophilized composition is a lyophilized cake with no melt back. In some cases, the lyophilized composition is a lyophilized cake with no collapse. In some cases, the residual water content of the lyophilized drug product is 5% or less, e.g., 4%, 3%, 2%, or 1% or less. In some cases, the residual water content is measured by Karl Fischer Titration, Thermogravimetric Analysis, Near Infra-red Spectroscopy, or Frequency Modulated Spectroscopy. In some cases, the residual water content is measured by Karl Fisher Titration. PREPARATION OF INJECTATE AND METHODS OF ADMINISTRATION Also described herein are methods of preparing an injectate from the lyophilized compositions described herein. In some cases, the method comprises reconstituting a lyophilized composition described herein in a pharmaceutically acceptable carrier, thereby producing an injectable composition. In some cases, the pharmaceutically acceptable carrier is water, e.g., bacteriostatic water for injection or sterile water for injection. In some cases, the pharmaceutically acceptable carrier is saline, e.g., isotonic saline, e.g., 0.9% saline. In some cases, the pH of the injectable solution is from 2 to 5, e.g., 2 to 4.5, 2 to 4, 2 to 3.5, 2 to 3, 2 to 2.5, 2.5 to 5, 2.5 to 4.5, 2.5 to 4, 2.5 to 3.5, 2.5 to 3, 3 to 5, 3 to 4.5, 3 to 4, 3 to 3.5, 3.5 to 5, 3.5 to 4.5, 3.5 to 4, 4 to 5, 4 to 4.5, or 4.5 to 5. In some cases, the injectable composition comprises 2.0 mg/ml or about 2.0 mg/ml of the peptide. In some cases, the injectable composition comprises 50 mg/ml or about 50 mg/ml of the bulking agent. In some cases, the reconstitution time in a pharmaceutically acceptable carrier (e.g., water or saline, e.g., 0.9% saline) is less than two minutes. In some cases, the injectable composition is a turbid solution with no visible residue, free from particles of foreign matter. Attorney Docket No.55002-0003WO1 In some cases, reconstituting the lyophilized composition comprises adding the pharmaceutically acceptable solution to a container comprising the lyophilized composition (e.g., an injection vial), inverting the vial a number of times (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 times), and holding the solution for a certain time (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29 or 30 minutes), at a certain temperature (e.g., room temperature or refrigeration temperature). In some cases, reconstituting further comprises shearing the reconstituted solution a number of times (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 times). In some cases, the sheared solution is held for a certain amount of time (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29 or 30 minutes) at a certain temperature (e.g., room temperature or refrigeration temperature). In some cases, the injectate is administered to a patient, e.g., a patient in need thereof. In some cases, the injectate is administered parenterally. In some cases, the injectate is administered locally, e.g., via local injection, e.g., via intraarticular or intralesional injection, e.g., via intradiscal injection. In some cases, the injectate is administered via epidural injection. In some cases, the injectate is administered to a joint or joints, e.g., by intra- articular injection and/or periarticular injection. In some cases, the joint is selected from a knee joint, a shoulder joint, a vertebral joint, a hip joint, a wrist joint, a hand joint, a finger joint, an ankle joint, a foot joint, a toe joint, or a combination thereof. In some cases, the joint is a facet joint. In some cases, the joint is a sacroiliac joint. In some cases, administration comprises reconstituting a lyophilized drug product described herein (e.g., as described herein) and administering it to a patient, e.g., as described herein. In some cases, the patient is a vertebrate. In some cases, the patient is a mammal. In some cases, the patient is a human. METHODS OF TREATMENT The peptides described herein find use as inhibitors of TGF-ȕ1 signaling. See, e.g., US Patent No.8,691,749, which is hereby incorporated by reference in its entirety; see also Kwon et al., “Anabolic Effects of Peniel 2000, a Peptide That Regulates TGF-ȕ1 Signaling on Intervertebral Disc Degeneration,” Spine 38(2):E49– E58 (2013). Therefore, in some cases, the patient has a disease or disorder that can be Attorney Docket No.55002-0003WO1 treated by inhibiting TGF-ȕ1 signaling (e.g., a disease or disorder characterized by overexpression of TGF-ȕ1). For example, degenerative disc diseases such as lumbar degenerative disc disease, body organ fibrosis, cancer, and/or glomerulosclerosis. As used in this context, to “treat” means to ameliorate at least one symptom of the disease or disorder. Thus, also provided herein are methods of treating a disease or disorder that can be treated by inhibiting TGF-ȕ1 signaling (e.g., degenerative disc diseases, body organ fibrosis, cancer, and/or flomerulosclerosis) in a patient, the method comprising administering the lyophilized compositions described herein or the injectable compositions described herein, e.g., a therapeutically effective amount of a lyophilized composition or injectable composition described herein, to the patient, e.g., as described herein. In some cases, the injectable composition is administered locally (e.g., as described herein). In some cases, administration antagonizes TGFȕ1 activity. In some cases, administration results in one or more of decreased inflammation, decreased pain, increased production of extracellular matrix, and improvement of the structural integrity of a diseased disc. Thus, also provided herein are methods for decreasing inflammation, decreasing joint pain, increasing production of extracellular matrix, and improving the structural integrity of a diseased disc, e.g., by administering the lyophilized compositions described herein or the injectable compositions described herein, e.g., a therapeutically effective amount of a lyophilized composition or injectable composition described herein, to the patient, e.g., as described herein. EXAMPLES The invention is further described in the following examples, which do not limit the scope of the invention described in the claims. Example 1: Preparation of Peptide The synthetic peptide LQVVYLH (SEQ ID NO: 2) was synthesized as a TFA salt, as described in Example 1 of 8,691,749, which is hereby incorporated by reference in its entirety. The peptide was formulated by two different manufacturing processes (A and B), to create two different formulations (A and B). Attorney Docket No.55002-0003WO1 Example 2: Formulation A / Manufacturing Process A For Process A, the peptide was manufactured as a low density free flowing lyophilized powder in a glass vial, without a bulking agent or other excipients (Formula A), and was then stoppered and sealed. To prepare an injectate, a second sterile vial containing 6.9% lactose (to give a 5% w/w lactose solution after re-constitution) and 0.9% saline was used to re- constitute. The injectate should contain 2 mg of peptide/ml of 5% lactose/0.9%wt% saline. Though, it was found that this process was not robust or scalable, due at least in part to the escape of peptide from vials during the lyophilization process. Example 3: Formulation B / Manufacturing Process B Because Process A (described in Example 2) was neither robust nor scalable, a new formulation, produced using a new manufacturing process (Process B, described in this example) was developed to produce a true lyophilized drug product that could be manufactured consistently, at large scale, for later reconstitution as an injectate. This process, summarized below, yielded a white lyophilized cake with no collapse or melt back. The process was both robust and scalable, and as described herein, surprisingly resulted in a dramatically improved shelf life as compared to Formulation A produced using Process A. Step 1 Formulation of 5% Lactose Solution To a 19 L pyrex carboy was charged 10 kg of WFI (water for injection) followed by lactose mono hydrate (632 g) and the resulting solution was stirred at room temperature at for NLT 30 minutes until dissolution was confirmed by visual inspection at which time the volume was adjusted to 12.19 kg (12 L) kg by addition of additional WFI. The density of solution was confirmed by IPC (1.016 g/ml; IPC range 1.014-1.019 g/ml). After the passing IPC, 8.00 kg of this 5% lactose solution was filtered through a Millipak 40, 0.22 micron filter (pre and post filter integrity confirmed by bubble point testing) into the 50 L Sterile Allegro Mixer while an additional 1.00 kg of solution was filtered through the Millipak 40, 0.22 micron filter into a clean glass bottle was used as necessary for the rinse during the peptide (SEQ ID NO: 2, prepared as described in Example 1) addition step. Attorney Docket No.55002-0003WO1 Step 2 Bulk Drug Product Formulation The 8.00 kg of 5% lactose solution in the 50 L Sterile Allegro Mixer was agitated and cooled to 5 +/- 3^oC at which time the peptide (approx.20 grams) was charged and the bottles and funnel were washed with a small portion of the 1.00 kg of filtered 5% lactose solution. The resulting solution (confirmed by visual inspection) was agitated for NMT 30 minutes at 5 +/- 3^oC and an IPC sample was taken to measure the concentration of the peptide solution by SoloVPE (target is NLT 2.0 mg/ml) and the pH (report value). If required, additional 5% lactose solution was charged in order to meet the final target concentration of 2.0

0.1 mg/ml, and this value was confirmed by a final IPC using SolvoVPE to confirm the necessary value. Step 3 Product Filtration and Vial Filling The drug product solution, still at 5 +/- 3^oC and under static conditions, was transferred from the Allegro Mixer to a 13 L glass carboy receiving vessel through two redundant Millipak 40, 0.22 micron sterilization filters. After filtration, the filters were tested for integrity via bubble point testing and the solution was tested for bioburden. Only after a passing result was confirmed for the filter integrity and bioburden was the solution carried on to the vial filling process. The sterile filtered peptide solution was filled into Schott 6R Top Lyo vials; 1.7 ml per vial (1.729 g based on solution density of 1.106g/ml), 3.4 mg of the peptide as TFA salt, 2.0 +/- 0.1 mg/ml) using a Chase Logeman filler operating at a speed of 45 vials per minute. Weight checks were performed every 100 vials for the first 600 vials and then ever 200 vials thereafter until the fill was complete with adjustments made as necessary until the fill was completed. Step 4 Lyophilization & Stoppering The filled and partially stoppered (20 mm Daikyou Flurotec V10F597W B2TR) vials were lyophilized using a Hull 280FXS450-SS20C lyophilizer. The filled vials were loaded into trays composed of 360 vials per tray. The batch was lyophilized using the lyophilization parameters outlined in Table 1. The vials were then fully stoppered and sealed under nitrogen using a GMP RW600 West capper and crimp sealed with a 20 mm FO white matte LQ TE 6-B 3766 seal. Attorney Docket No.55002-0003WO1 Table 1 Lyophilization Cycle and Parameters

Step 5 Sampling, Inspection and Packaging The drug product vials are single dose units of 3 mg/vial of the peptide (as a TFA salt), with overfill to 3.4 mg, as a lyophilized cake (with <2% w/w residual water content), designed to be reconstituted with 1.7 ml of 0.9% saline to provide a 1.5 ml solution of approximately 2.0 mg/ml of peptide at a pH of 2.5-4.0, for injection. The drug product vials were visually inspected for defects and then packaged in corrugated boxes and placed in 2-8^oC storage to await final release and shipment for clinical labeling and kitting. The final drug product composition is as follows: Table 2. Drug Product Composition

Attorney Docket No.55002-0003WO1

The lyophilized drug produced had the following properties: Table 3. Drug Product Properties

Example 4: Stability In addition to the benefits of being able to manufacture with Process B consistently and at large scale, it was found that, surprisingly, the stability of Formulation B was dramatically increased compared to Formulation A, including when stored at or above 5°C (e.g., at 25°C and 40°C). Stability of Formulation A The stability of three different lots of Formulation A, produced according to Process A described in Example 2, was tested for stability at 25°C ± 2°C/ 60% ± 5% Relative Humidity (RH), 5°C ± 3°C, and -20°C ± 5°C. An UPLC method with ultraviolet (UV) detection was used to determine the identity, assay, and content of related organic impurities, including degradation products. The assay content is determined by external standard quantitation using a reference standard, while impurities were reported according to area percent normalization. Table 4. Stability of Formulation A

Attorney Docket No.55002-0003WO1

NM = not measured Stability of Formulation B Four different lots were manufactured, at 2.3 L, 10L, 8 L and 10 L scale, and placed on a 36-month ICH stability program at -20°C and 2-8°C (5°C) and additional stress conditions of 25°C/60% RH and 40°C/75% RH. Assay (expressed as the peptide amount in mg/ml when reconstituted to the intended injectate volume for Batches 1–3 and as the % of the intended peptide concentration when reconstituted to the intended injectate volume for Batch 4) and degradation product content were determined by a gradient ultra high-performance liquid chromatography (UHPLC) method. Samples were prepared by adding 1.7 mL water to the vial and after ensuring complete dissolution, further diluting to a working concentration of 1 mg/mL peptide. The strength of each vial was determined by external peptide standard quantitation. Any peaks observed above the reporting threshold are quantified against the external standard to yield degradation product results as weight percent. A summary of stability batch information gathered is provided in Table 5. To show comparability between different peptide manufacturers, batch 1 was produced Attorney Docket No.55002-0003WO1 from peptide from one manufacturer, and batches 2 and 3 were produced from another manufacturer. As shown through an evaluation of the data, there are no differences in quality or stability of the drug product batches manufactured, regardless of the drug substance source. Total moisture content (%w/w) remained below 2% under all conditions. Reconstitution time in 1.7 ml 0.9% saline was less than two minutes under all conditions. Table 5 Summary of Stability Batch Information for Formulation B

Table 6 Stability of Formulation B (Batches 1–3)

Attorney Docket No.55002-0003WO1

NM = not measured Batch 4 was also tested for stability after 9 months at 5°C and 6 months at 25°C/60% RH. Table 7 Stability of Formulation B (Batch 4)

Stability of Formulation B—Batch 4, Prepared Injectate The lyophilate was reconstituted in saline and held in vials or syringes at 5 or 25 °C for up to 24 hours. Samples were tested for appearance, pH, solubility by UV- VIS spectrophotometry (A280), and content and purity by UPLC. To determine vial- Attorney Docket No.55002-0003WO1 to-vial consistency, 18 vials were assessed at T0. Other time-points were analyzed in multiplicate. Analytical results were highly consistent across each vial tested and the results presented below are based on the mean. Table 8 pH and Solubility of Injectate

Table 9 Stability of Injectate

Attorney Docket No.55002-0003WO1 Summary of Stability Studies Results from the stability studies indicate that, unlike Formula A, Formula B is stable when stored at either 2-8°C (5°C) for twelve months and at accelerated conditions, including at 25°C/60% RH for six months and at 40°C/75% RH for 1 month. Example 5: Preparation of Injectate The lyophilized drug product prepared according to Example 3 was packaged into vials at 3 mg/vial (with overfill, as described in Example 3), and reconstituted in 0.9wt% saline, for a final injectate of 2 mg of peptide per milliliter, with 5% lactose and 0.9wt% saline. Example 6: Further Characterization of Formula B The stability of the three development lots of final drug product (FDP) was assessed in support of early phase development stability related to shelf life. Stability of peptide FDP was evaluated as lyophilized cakes, and reconstituted in WFI (pH, TFA content, lactose content, content and purity, and HIAC) and saline (pH, % Remedisc solubility, and FlowCam) for 24 months when stored at -80 ȗC, -20 ȗC, 5 ȗC, 25 ȗC, and 40 ȗC. Table 12 provides the testing schedule for the 3 development lots, where the accelerated condition of 40 ȗC was evaluated for 6 months. Assays executed at each timepoint can be found in Table 13. 100% visual inspection of lyophilized cakes were executed at T0. Only those cakes that met the following criteria were placed on stability: white cake, no melt-bac, proper container closure, target fill achieved (no over or under filled), non- thermocoupled vials, and no cracking. During the stability study, vials that were pulled at each timepoint and storage condition were inspected. Cake appearance for each development lot remained unchanged at all evaluated timepoints and conditions, consistent with the following description: “white powder with no reduction in cake height or evidence of melt-back or internal collapse.” Attorney Docket No.55002-0003WO1 Development lot cake characteristics including moisture content, cake Tg, cake structure (SEM), and reconstitution time and appearance were evaluated according to the testing plan in Table 13. Moisture content increased significantly during storage at 5 °C, 25 °C, and 40 °C, while cake Tg decreased during storage at these temperatures. An investigation showed that these changes are related to the transfer of residual moisture from the stopper to the lyophilized drug product cake. Additional drying for stoppers can be implemented to reduce risk of stopper moisture transfer to the drug product cake. Preliminary stability data from such batches indicates stable moisture content that remains with the specification limit. Cake structure by SEM and cake reconstitution time were consistent over time for all lots and conditions evaluated, showing no meaningful trends. Residual moisture in lyophilized cakes from all three development lots was evaluated by Karl Fisher titration. Residual moisture data from T0 and all subsequent evaluated timepoints was less than 2%. A small but statistically significant increase in moisture content was observed across all three development lots when FDP vials were stored at 5 ȗC, 25 ȗC, and 40 ȗC. Results of an investigation suggest that this trend is due to the hygroscopic nature of the lyophilized product drawing moisture retained in the stopper back into the lyophilized FDP. While the observed increases are small (all MC results remain below 2%), to mitigate the risk of impact to FDP stability, an additional drying can be incorporated when autoclaving the stoppers. Preliminary data from additional lots in which stoppers are autoclaved indicates stable moisture content, as shown in Table 10. Table 10: Moisture content for additional peptide lots

Associated with the increase in moisture content was a decrease in Tg. A significant reduction in Tg was observed for all three development lots when stored at 5 ÛC, 25 ÛC, and 40 ÛC. Related to the increase in moisture content, the reduction in cake Tg is most likely driven by moisture retained in the stopper being drawn into the Attorney Docket No.55002-0003WO1 lyophilized FDP. Tg for lactose is known to be highly correlated with moisture content (see, e.g. Drake, Andrew C et al. “Effect of water content on the glass transition temperature of mixtures of sugars, polymers, and penetrating cryoprotectants in physiological buffer.” PloS one vol.13,1 e0190713.5 Jan.2018, doi:10.1371/journal.pone.0190713). Analysis of the pooled Tg and moisture content data from the three peptide development lots shows the expected highly significant negative correlation between moisture content and decreasing Tg (p<0.001, R²= 0.797). Peptide FDP vials stored at 5 ÛC begin to approach a Tg of 90 ÛC as early as 24-months. Additional drying during the stopper autoclave cycle reduces moisture retained in the stopper and preserves the higher Tg observed at T0. To eliminate the possibility that the observed moisture content / Tg changes were driven by a Maillard reaction, placebo vials (5% lactose monohydrate) were placed under accelerated stability conditions for 14 days. The Tg of the placebo vials reduced, demonstrating that the trend is not driven by an interaction between the reducing sugar lactose and the API. To confirm that reduction in Tg was driven by residual moisture retained in the rubber stoppers, peptide FDP vials were stored at 25 ÛC, or 40 ÛC in the presence of an increasing number of rubber stoppers (0-4). Thermal analysis of Tg after 3 days demonstrated that overall, the rate of Tg reduction was greatest with a larger number of stoppers (Table 11). The apparent reduction in Tg when peptide FDP is stored with 0 stoppers is likely caused by an incomplete seal of the adhesive foil. Table 11: Thermal analysis of peptide FDP when stored with varying stopper numbers

Attorney Docket No.55002-0003WO1

FDP cakes were evaluated quantitatively by SEM for skin thickness and qualitatively for cake structure (top, middle, and bottom). No meaningful trends were observed for skin thickness across all 3 developments lots and storage conditions, with skin thickness measuring between 10.7 and 21.7 μm. No differences were observed when evaluating internal cake structure by SEM. This analysis involved qualitatively scaling cake structure on a scale of 1-5, where 1 represents poor cake structure with collapse and 5 represents an ideal uniform honeycomb structure. Reconstitution time in in WFI for all three development lots was less than two minutes at all evaluated timepoints and conditions with no meaningful trends observed. Development lot reconstituted final drug product characteristics including pH (through T9m only), TFA content, lactose content, peptide content and purity by UPLC, and HIAC, were reconstituted in WFI and evaluated according to the testing plan in Table 13. Development lot reconstituted drug product characteristics including % peptide solubility, FlowCam, and pH (beginning at T12m) were reconstituted in 0.9% saline and evaluated according to the testing plan in Table 13. Table 12: Development Lots FDP Stability Testing Schedule

1-80 ÛC stability vials were only evaluated for key assays at later timepoints (moisture content, Tg by DSC, and UPLC); NT= not tested Attorney Docket No.55002-0003WO1 Table 13: Development Lots FDP Stability Assays

140 ÛC only; NT= not tested A reduction in the % purity of the peptide by UPLC was observed for final drug product (FDP) vials stored at 25 ȗC and 40 ȗC for all three development lots. At the observed rates of change for FDP vials stored at 25 ȗC and 40 ȗC, peptide % purity by UPLC could approach 98% within 30 to 70 months at 25 °C or 6 to 8 months at 40 °C. This data indicates that short-term exposure to ambient temperature (e.g. during inspection, packaging, clinical handling, etc.) is likely low risk. Peptide purity at -80 °C, -20 °C, and 5 °C showed no meaningful trends for the three development lots. For other product characteristics tested, including pH, TFA content, lactose content, peptide content, and particle size distribution by FlowCam and HIAC, no meaningful trends for any storage temperature were observed. Attorney Docket No.55002-0003WO1 Peptide content and % purity were evaluated by UPLC, and overall the data supports long-term storage of the peptide FDP at 5 ȗC. Content remained within 90-110% of 2.0 mg/mL (observed range 1.84-2.22 mg/mL) at all tested conditions and timepoints, and no meaningful trends were observed. Drug product target profile was met for % purity at all tested conditions and timepoints (% purity NLT 98%), and no meaningful trends were observed when peptide FDP vials were stored at -80 ȗC, -20 ȗC, or 5 ȗC. A statistically significant and reduction in % purity was observed when peptide FDP vials were stored at 25 ȗC and 40 ȗC, and regression analysis was performed (Table 14). Extrapolation using the 95% confidence interval of the observed slope suggests that the % purity approaches the lower limit of the specification range (NLT 98%) as soon as 30 months when stored at 25 ȗC, and as soon as 6 months when stored at 40 ȗC. Table 14: Statistical analysis of % purity for development lots

Attorney Docket No.55002-0003WO1

NT = not tested Analysis of additional FDP characteristics including pH, % peptide solubility, PSD by FlowCam, and HIAC, revealed no meaningful trends indicating risk to product at a storage condition of 5 ȗC.

Attorney Docket No.55002-0003WO1 OTHER EMBODIMENTS It is to be understood that while the invention has been described in conjunction with the detailed description thereof, the foregoing description is intended to illustrate and not limit the scope of the invention, which is defined by the scope of the appended claims. Other aspects, advantages, and modifications are within the scope of the following claims.

Claims

Attorney Docket No.55002-0003WO1 WHAT IS CLAIMED IS: 1. A lyophilized composition comprising: a peptide comprising or consisting of the amino acid sequence SGLPDLKLLQVVYLHSNNI (SEQ ID NO: 20) or fragment thereof (e.g., 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, or 18 consecutive amino acids of SEQ ID NO: 20), optionally with one or more conservative amino acid substitutions, or a salt thereof, optionally a pharmaceutically acceptable salt; and a bulking agent. 2. The lyophilized composition of claim 1, wherein the peptide or pharmaceutically acceptable salt thereof comprises or consists of the amino acid sequence L-X1-V-V-X2-L-X3, (SEQ ID NO: 1), where X1 is Q or N; X2 is Y, F, or W; X3 is H, K, or R; L is Leucine; Q is Glutamine, N is Asparagine, V is Valine, Y is Tyrosine, F is Phenylalanine, W is Tryptophan, H is Histidine, K is Lysine, and R is Arginine. 3. The lyophilized composition of claim 2, wherein the peptide comprises or consists of an amino acid sequence selected from the group consisting of LQVVYLH (SEQ ID NO: 2), LQVVYLK (SEQ ID NO: 3), LQVVYLR (SEQ ID NO: 4), LQVVFLH (SEQ ID NO: 5), LQVVFLK (SEQ ID NO: 6), LQVVFLR (SEQ ID NO: 7), LQVVWLH (SEQ ID NO: 8), LQVVWLK (SEQ ID NO: 9), LQVVWLR (SEQ ID NO: 10), LNVVYLH (SEQ ID NO: 11), LNVVYLK (SEQ ID NO: 12), LNVVYLR (SEQ ID NO: 13), LNVVFLH (SEQ ID NO: 14), LNVVFLK (SEQ ID NO: 15), LNVVFLR (SEQ ID NO: 16), LNVVWLH (SEQ ID NO: 17), LNVVWLK (SEQ ID NO: 18), LNVVWLR (SEQ ID NO: 19), and combinations thereof. 4. The lyophilized composition of claim 3, wherein the peptide comprises LQVVYLH (SEQ ID NO: 2). 5. The lyophilized composition of claim 3, wherein the peptide consists of LQVVYLH (SEQ ID NO: 2). Attorney Docket No.55002-0003WO1 6. The lyophilized composition of any one of claims 1–5, wherein the peptide consists of an amino acid sequence that is less than 50 amino acids in length, optionally between 7 and 10 amino acids in length. 7. The lyophilized composition of any one of claims 1–6, wherein the peptide is formulated as a pharmaceutically acceptable salt. 8. The lyophilized composition of claim 7, wherein the salt is an acid salt. 9. The lyophilized composition of claim 8, wherein the salt is a trifluoracetic acid salt, an acetate salt, a hydrochloride salt, or a combinations thereof. 10. The lyophilized composition of claim 9, wherein the salt is a trifluoracetic acid salt. 11. The lyophilized composition of any one of claims 1–10, wherein the peptide is an inhibitor of TGF-ȕ1 signaling. 12. The lyophilized composition of any one of claims 1–11, wherein the bulking agent is selected from lactose (e.g., lactose monohydrate), sucrose, lactose, trehalose, mannitol, sorbitol, glucose, rafinose, glycine, histidine, polyethylene glycol, polyvinyl pyrollidone, bovine serum albumin, dextran, and combinations thereof. 13. The lyophilized composition of claim 12, wherein the bulking agent is lactose monohydrate. 14. The lyophilized composition of any one of claims 1–13, consisting essentially of the peptide and the bulking agent. 15. The lyophilized composition of any one of claims 1–13, consisting of the peptide, the bulking agent, and 5% wt/wt or less residual water. 16. The lyophilized composition of any one of claims 1–13, consisting of the peptide, the bulking agent, and 2% wt/wt or less residual water. Attorney Docket No.55002-0003WO1 17. The lyophilized composition of any one of claims 1–13, consisting of the peptide, the bulking agent, and 1% wt/wt or less residual water. 18. The lyophilized composition of any one of claims 1–17, comprising from 1% to 10% wt/wt of the peptide. 19. The lyophilized composition of claim 18, comprising from 2% to 5% wt/wt of the peptide. 20. The lyophilized composition of claim 19, comprising from 3.8% to 3.9% wt/wt of the peptide. 21. The lyophilized composition of any one of claims 1–14 or 18–20, wherein the residual water content is 5% wt/wt or less. 22. The lyophilized composition of claim 21, wherein the residual water content is 2% wt/wt or less. 23. The lyophilized composition of claim 22, wherein the residual water content is 1% wt/wt or less. 24. The lyophilized composition of any one of claims 15–23, wherein the residual water content is measured by Karl Fischer Titration, Thermogravimetric Analysis, Near Infra-red Spectroscopy, or Frequency Modulated Spectroscopy. 25. The lyophilized composition of claim 24, wherein the residual water content is measured by Karl Fisher Titration. 26. A container comprising the composition of any one of claims 1–25. 27. The container of claim 26, wherein the container is a plastic container or a glass container. 28. The container of claim 27, wherein the plastic container is a polystyrene container or a polypropylene container. Attorney Docket No.55002-0003WO1 29. The container of any one of claims 26–28, wherein the container is translucent or clear. 30. The container of any one of claims 26–29, wherein the container is chemically resistant or chemically inert. 31. The container of any one of claims 26–30, wherein the container is a vial. 32. The container of claim 31, wherein the vial is an injection vial. 33. The container of claim 32, wherein the vial is a glass injection vial. 34. The container of claim 33, wherein the glass injection vial comprises a hydrophobic inner coating. 35. The container of claim 34, wherein the hydrophobic inner coating is a chemically uniform hydrophobic inner coating. 36. The container of claim 34 or claim 35, wherein the hydrophobic inner coating is a Si-O-C-H coating. 37. The container of any one of claims 34–36, wherein the hydrophobic inner coating is about 40 nm thick. 38. The container of any one of claims 34–37, wherein the coating is bonded covalently to the glass substrate. 39. The container of claim 33, wherein the glass injection vial does not comprise a hydrophobic inner coating. 40. The container of any one of claims 26–38, further comprising a stopper. 41. The container of claim 40, wherein the stopper comprises a barrier film. 42. The container of claim 41, wherein the barrier film is chemically inert. Attorney Docket No.55002-0003WO1 43. The container of claim 41 or 42, wherein the barrier film is a fluoropolymer film. 44. The container of claim 43, wherein the fluoropolymer film is a poly(ethylene tetrafluoroethylene) (ETFE) fluoropolymer film. 45. The container of claim 40, wherein the stopper does not comprise a barrier film. 46. The container of any one of claims 26–45, wherein the container has a volume capacity of from 2 ml to 100 ml. 47. The container of claim 46, wherein the container is a 6 ml injection vial. 48. The container of any one of claims 26–47, wherein the container contains from 10 to 500 mg of the composition. 49. The container of claim 48, wherein the container contains from 78 to 100 mg of the composition. 50. The container of claim 49, wherein the container contains from 78 to 89 mg of the composition. 51. The container of any one of claims 26–50, wherein the container comprises at least 78 mg of the composition. 52. The composition of any one of claims 1-25, or the container of any one of claims 26-51, wherein the lyophilized composition is stable for at least 1 month at 25°C ± 2°C. 53. The composition or container of claim 52, wherein the lyophilized composition is stable for at least 1 month at 25°C ± 2°C / 60% ± 5% Relative Humidity. Attorney Docket No.55002-0003WO1 54. The composition of any one of claims 1-25, or the container of any one of claims 26-51, wherein the lyophilized composition is stable for at least 1 month at 40°C ± 2°C. 55. The composition of any one of claims 1-25, or the container of any one of claims 26-51, wherein the lyophilized composition is stable for at least 1 month at 5°C ± 3°C. 56. The composition or container of any one of claims 52–54, wherein the lyophilized composition is stable for at least 2 months. 57. The composition or container of claim 56, wherein the lyophilized composition is stable for at least 3 months. 58. The composition of claim 57, wherein the lyophilized composition is stable for at least 6 months. 59. The composition or container of any one of claims 52–58, wherein the composition is stable if the proportion of peptide in the composition does not decrease, or decreases by no more than 5%. 60. The composition or container of claim 59, wherein the composition is stable if the proportion of peptide in the composition does not decrease, or decreases by no more than 2%. 61. The composition or container of claim 60, wherein the composition is stable if the proportion of peptide in the composition does not decrease, or decreases by no more than 1%. 62. The composition or container of any one of claims 52–58, wherein the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 0.5%. Attorney Docket No.55002-0003WO1 63. The composition or container of claim 62, wherein the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 1%. 64. The composition or container of claim 62, wherein the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 2%. 65. The composition or container of claim 64, wherein the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 5%. 66. The composition or container of any one of claims 59–65, wherein the proportion of peptide in the composition or the proportion of degradation product(s) in the composition is measured by liquid chromatography. 67. The composition or container of claim 66, wherein the liquid chromatography is ultra high-performance liquid chromatography (UPLC). 68. The composition or the container of any one of claims 1–65, wherein the composition is white to off white. 69. The composition or container of any one of claims 1–68, wherein the composition is a lyophilized cake with no melt back. 70. The composition or container of any one of claims 1–69, wherein the composition is a lyophilized cake with no collapse. 71. A method for producing a lyophilized composition comprising a peptide comprising or consisting of the amino acid sequence SGLPDLKLLQVVYLHSNNI (SEQ ID NO: 20) or fragment thereof (e.g., 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, or 18 consecutive amino acids of SEQ ID NO: 20), optionally with one or more conservative amino acid substitutions, or a pharmaceutically acceptable salt thereof, and a bulking agent, the method comprising: Attorney Docket No.55002-0003WO1 preparing or having prepared a solution comprising the peptide and the bulking agent; and lyophilizing the solution. 72. The method of claim 71, wherein the peptide comprises or consists of the amino acid sequence L-X1-V-V-X2-L-X3, (SEQ ID NO: 1), where X1 is Q or N; X2 is Y, F, or W; X₃ is H, K, or R; L is Leucine; Q is Glutamine, N is Asparagine, V is Valine, Y is Tyrosine, F is Phenylalanine, W is Tryptophan, H is Histidine, K is Lysine, and R is Arginine. 73. The method of claim 72, wherein the peptide comprises or consists of an amino acid sequence selected from the group consisting of LQVVYLH (SEQ ID NO: 2), LQVVYLK (SEQ ID NO: 3), LQVVYLR (SEQ ID NO: 4), LQVVFLH (SEQ ID NO: 5), LQVVFLK (SEQ ID NO: 6), LQVVFLR (SEQ ID NO: 7), LQVVWLH (SEQ ID NO: 8), LQVVWLK (SEQ ID NO: 9), LQVVWLR (SEQ ID NO: 10), LNVVYLH (SEQ ID NO: 11), LNVVYLK (SEQ ID NO: 12), LNVVYLR (SEQ ID NO: 13), LNVVFLH (SEQ ID NO: 14), LNVVFLK (SEQ ID NO: 15), LNVVFLR (SEQ ID NO: 16), LNVVWLH (SEQ ID NO: 17), LNVVWLK (SEQ ID NO: 18), LNVVWLR (SEQ ID NO: 19), and combinations thereof. 74. The method of claim 73, wherein the peptide comprises LQVVYLH (SEQ ID NO: 2). 75. The method of claim 73, wherein the peptide consists of LQVVYLH (SEQ ID NO: 2). 76. The method of any one of claims 71–75, wherein the peptide consists of an amino acid sequence that is less than 50 amino acids in length, optionally between 7 and 10 amino acids in length. 77. The method of any one of claims 71–76, wherein the peptide is formulated as a pharmaceutically acceptable salt. 78. The method of claim 77, wherein the salt is an acid salt. Attorney Docket No.55002-0003WO1 79. The method of claim 78, wherein the salt is a trifluoracetic acid salt, an acetate salt, a hydrochloride salt, or a combinations thereof. 80. The method of claim 79, wherein the salt is a trifluoracetic acid salt. 81. The method of any one of claims 71–80, wherein the peptide is an inhibitor of TGF-ȕ1 signaling. 82. The method of any one of claims 71–81, wherein the bulking agent is selected from lactose (e.g., lactose monohydrate), sucrose, lactose, trehalose, mannitol, sorbitol, glucose, rafinose, glycine, histidine, polyethylene glycol, polyvinyl pyrollidone, bovine serum albumin, dextran, and combinations thereof. 83. The method of claim 82, wherein the bulking agent is lactose monohydrate. 84. The method of any one of claims 71–83, wherein preparing or having prepared a solution comprising the peptide and the bulking agent comprises: preparing the peptide or having the peptide prepared; preparing or having prepared a solution comprising the bulking agent; and mixing the peptide and the solution comprising the bulking agent. 85. The method of claim 84, wherein preparing the peptide or having the peptide prepared comprises synthesizing the peptide or having the peptide synthesized. 86. The method of claim 84 or 85, wherein the peptide is lyophilized. 87. The method of any one of claims 84–86, wherein preparing or having prepared a solution comprising the bulking agent comprises: mixing the bulking agent with water or an aqueous solution. 88. The method of claim 87, wherein preparing or having prepared a solution comprising the bulking agent comprises: mixing the bulking agent with water. Attorney Docket No.55002-0003WO1 89. The method of claim 87 or 88, further comprising filtering the solution comprising the bulking agent. 90. The method of any one of claims 84–89, wherein the solution comprising the bulking agent comprises from 4 to 6% w/w of the bulking agent. 91. The method of claim 89, wherein the solution comprising the bulking agent comprises from 4.5 to 5.5% w/w of the bulking agent. 92. The method of claim 91, wherein the solution comprising the bulking agent comprises 5% w/w of the bulking agent or about 5% w/w of the bulking agent. 93. The method of any one of claims 73 to 92, wherein the solution comprising the peptide and the bulking agent comprises from 1.5 to 2.5 mg/ml of the peptide. 94. The method of claim 93, wherein the solution comprising the peptide and the bulking agent comprises from 1.9 to 2.1 mg/ml of the peptide. 95. The method of any one of claims 71–94, wherein the pH of the solution comprising the peptide and the bulking agent is, or is adjusted to, 2–5. 96. The method of claim 95, wherein the pH of the solution comprising the peptide and the bulking agent is, or is adjusted to, 2.5–4. 97. The method of claim 96, wherein the pH of the solution comprising the peptide and the bulking agent is, or is adjusted to, 3 or about 3. 98. The method of any one of claims 84–97, wherein mixing the peptide and the solution comprising the bulking agent comprises agitation for 30 minutes or less. 99. The method of claim 98, wherein mixing the peptide and the solution comprising the bulking agent comprises agitation at 5 ± 3°C. 100. The method of any one of claims 71–99, further comprising filtering the solution comprising the peptide and the bulking agent. Attorney Docket No.55002-0003WO1 101. The method of any one of claims 71–100, further comprising dispensing all or a portion of the solution comprising the peptide and the bulking agent into one or more container(s). 102. The method of claim 101, wherein the container is a plastic container or a glass container. 103. The method of claim 102, wherein the plastic container is a polystyrene container or a polypropylene container. 104. The method of any one of claims 101–103, wherein the container is translucent or clear. 105. The method of any one of claims 101–104, wherein the container is chemically resistant or chemically inert. 106. The method of any one of claims 101–105, wherein the container is a vial. 107. The method of 106, wherein the vial is an injection vial. 108. The method of claim 107, wherein the vial is a glass injection vial. 109. The method of claim 108, wherein the glass injection vial comprises a hydrophobic inner coating. 110. The method of claim 109, wherein the hydrophobic inner coating is a chemically uniform hydrophobic inner coating. 111. The method of claim 109 or claim 110, wherein the hydrophobic inner coating is a Si-O-C-H coating. 112. The method of any one of claims 109–111, wherein the hydrophobic inner coating is about 40 nm thick. Attorney Docket No.55002-0003WO1 113. The method of any one of claims 109–112, wherein the coating is bonded covalently to the glass substrate. 114. The method of claim 108, wherein the glass injection vial does not comprise a hydrophobic inner coating. 115. The method of any one of claims 101–113, wherein the container has a volume of from 2 ml to 100 ml. 116. The method of claim 115, wherein the container is a 6 ml injection vial. 117. The method of any one of claims 101–116, wherein dispensing all or a portion of the solution comprising the peptide and the bulking agent into a container comprises dispensing from 1.0 to 2.0 ml of the solution into the container. 118. The method of claim 117, wherein dispensing all or a portion of the solution comprising the peptide and the bulking agent into a container comprises dispensing 1.7 ml or about 1.7 ml into the container. 119. The method of any one of claims 101–118, wherein dispensing all or a portion of the solution comprising the peptide and the bulking agent into a container comprises dispensing a volume of the solution comprising from 2.5 mg to 3.5 mg of the peptide into the container. 120. The method of claim 119, wherein dispensing all or a portion of the solution comprising the peptide and the bulking agent into a container comprises dispensing a volume of the solution comprising 3.0 mg or about 3.0 mg of the peptide into the container. 121. The method of any one of claims 101–120, wherein the solution is dispensed into more than one container, optionally 100 or more containers, 500 or more, 1,000 or more, 5,000 or more, or 10,000 or more containers. 122. The method of any one of claims 101–121, wherein the solution is dispensed at a rate of from 10 to 100 containers per minute. Attorney Docket No.55002-0003WO1 123. The method of any one of claims 101–122, wherein the solution is dispensed at a rate of at least 10 containers per minute, optionally at least 20, 30, or 40 containers per minute. 124. The method of any one of claims 101–123, further comprising partially stoppering the filled container with a stopper. 125. The method of claim 124, wherein the stopper comprises a barrier film. 126. The method of claim 125, wherein the barrier film is chemically inert. 127. The method of claim 125 or 126, wherein the barrier film is a fluoropolymer film. 128. The method of claim 127, wherein the fluoropolymer film is a poly(ethylene tetrafluoroethylene) (ETFE) fluoropolymer film. 129. The method of claim 124, wherein the stopper does not comprise a barrier film. 130. The method of any one of claims 71–129, wherein lyophilizing the solution comprises, in sequence: 1) a freezing stage; 2) a primary drying stage; and 3) a secondary drying stage. 131. The method of claim 130, wherein the freezing stage comprises, in sequence: 1) a loading step; 2) a first freezing step; 3) an annealing step; and 4) a second freezing step. 132. The method of claim 131, wherein the loading step comprises placing containers comprising the solution into a lyophilizer chamber, optionally at 5°C or about 5°C, optionally under atmospheric pressure. Attorney Docket No.55002-0003WO1 133. The method of claim 131 or claim 132, wherein the first freezing step comprises decreasing the temperature of the chamber to -50°C or to about -50°C under atmospheric pressure over the course of a ramp period, and holding the chamber at that temperature for a soak period, optionally wherein the ramp period is 55 minutes or about 55 minutes, and optionally wherein the soak period is 150 minutes or about 150 minutes. 134. The method of any one of claims 131–133, wherein the annealing step comprises increasing the temperature of the chamber to -10°C or about -10°C under atmospheric pressure over the course of a ramp period, and holding the chamber at that temperature for a soak period, optionally wherein the ramp period is 40 minutes or about 40 minutes, and optionally wherein the soak period is 150 minutes or about 150 minutes. 135. The method of any one of claims 131–134, wherein the first freezing step comprises decreasing the temperature of the chamber to -50°C or to about -50°C under atmospheric pressure over the course of a ramp period, and holding the chamber at that temperature for a soak period, optionally wherein the ramp period is 40 minutes or about 40 minutes, and optionally wherein the soak period is 120 minutes or about 120 minutes. 136. The method of any one of claims 130–135, wherein the primary drying stage comprises, in sequence: 1) decreasing the pressure of the chamber to 75 mTorr or about 75 mTorr while holding the temperature steady at -50°C or to about -50°C, and holding the chamber at that pressure and temperature for a soak period, optionally wherein the soak period is 60 minutes or about 60 minutes; and 2) increasing the temperature of the chamber to -15°C or about -15°C and holding the pressure of the chamber steady at 75 mTorr or about 75 mTorr over the course of a ramp period, and holding the chamber at that temperature and pressure for a soak period, optionally wherein the ramp period is 35 minutes or about 35 minutes, and optionally wherein the soak period is 2184 minutes or about 2184 minutes. Attorney Docket No.55002-0003WO1 137. The method of any one of claims 130–136, wherein the secondary drying stage comprises raising the temperature of the chamber to 5°C or about 5°C and holding the pressure of the chamber steady at 75 mTorr or about 75 mTorr over the course of a ramp period, and holding the chamber at that temperature and pressure for a soak period, optionally wherein the ramp period is 180 minutes or about 180 minutes, and optionally wherein the soak period is 600 minutes or about 600 minutes. 138. The method of any one of claims 101–137, further comprising back-filling the containers with an inert gas and fully stoppering with a stopper. 139. The method of claim 138, wherein the inert gas is nitrogen. 140. The method of claim 138 or 139, wherein back-filling the containers with an inert gas and fully stoppering with a stopper is carried out at 5°C or about 5°C, optionally at 600,000 mTorr or about 600,000 mTorr. 141. The method of any one of claims 138–140, wherein the stopper comprises a barrier film. 142. The method of claim 141, wherein the barrier film is chemically inert. 143. The method of claim 141 or 142, wherein the barrier film is a fluoropolymer film. 144. The method of claim 143, wherein the fluoropolymer film is a poly(ethylene tetrafluoroethylene) (ETFE) fluoropolymer film. 145. The method of any one of claims 101–144, wherein the method comprises partially stoppering the filled container with a stopper according to any one of claims 124–129, and wherein the container and stopper comprising the solution comprising the peptide and the bulking agent are the same as the container and stopper comprising the lyophilized solution comprising the peptide and the bulking agent. 146. The method of any one of claims 101–145, further comprising sealing the container. Attorney Docket No.55002-0003WO1 147. The method of claim 146, wherein the container is sealed with a flip-off seal. 148. The method of any one of claims 101–147, further comprising one or more of: inspecting, packaging, shipping, storing or labeling the container(s). 149. A lyophilized composition produced according to the method of any one of claims 71–148. 150. The lyophilized composition of claim 148, wherein the lyophilized composition is stable for at least 1 month at 25°C ± 2°C. 151. The lyophilized composition of claim 150, wherein the lyophilized composition is stable for at least 1 month at 25°C ± 2°C / 60% ± 5% Relative Humidity. 152. The lyophilized composition of claim 148, wherein the lyophilized composition is stable for at least 1 month at 40°C ± 2°C. 153. The lyophilized composition of any one of claims 148–152, wherein the lyophilized composition is stable for at least 2 months. 154. The composition of claim 153, wherein the lyophilized composition is stable for at least 3 months. 155. The composition of claim 154, wherein the lyophilized composition is stable for at least 6 months. 156. The composition of any one of claims 150–155, wherein the lyophilized composition is stable if the proportion of peptide in the composition does not decrease, or decreases by no more than 5%. 157. The composition or container of claim 156, wherein the composition is stable if the proportion of peptide in the composition does not decrease, or decreases by no more than 2%. Attorney Docket No.55002-0003WO1 158. The composition or container of claim 157, wherein the composition is stable if the proportion of peptide in the composition does not decrease, or decreases by no more than 1%. 159. The composition or container of any one of claims 150–158, wherein the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 0.5%. 160. The composition or container of claim 159, wherein the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 1%. 161. The composition or container of claim 160, wherein the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 2%. 162. The composition or container of claim 161, wherein the composition is stable if the proportion of degradation product(s) in the composition does not increase, or increases by no more than 5%. 163. The composition or container of any one of claims 156–162, wherein the proportion of peptide in the composition or the proportion of degradation product(s) in the composition is measured by liquid chromatography. 164. The composition or container of claim 163, wherein the liquid chromatography is ultra high-performance liquid chromatography (UPLC). 165. The composition of any one of claims 149–164, wherein the composition is white to off white. 166. The composition or container of any one of claims 149–165, wherein the composition is a lyophilized cake with no melt back. 167. The composition or container of any one of claims 149–166, wherein the composition is a lyophilized cake with no collapse. Attorney Docket No.55002-0003WO1 168. Use of a peptide a peptide comprising or consisting of the amino acid sequence SGLPDLKLLQVVYLHSNNI (SEQ ID NO: 20) or fragment thereof (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, or 18 consecutive amino acids of SEQ ID NO: 20), optionally with one or more conservative amino acid substitutions, or pharmaceutically acceptable salt thereof; and/or a bulking agent in the production of a lyophilized composition comprising the peptide and the bulking agent. 169. A method for producing an injectable composition, the method comprising: reconstituting the lyophilized composition of any one of claims 1–25, 52–70 or 149–156, or the lyophilized composition within the container of any one of claims 26–70 in a pharmaceutically acceptable carrier, thereby producing an injectable composition. 170. The method of claim 169, wherein the pharmaceutically acceptable carrier is water or saline. 171. The method of claim 170, wherein the pharmaceutically acceptable carrier is saline. 172. The method of claim 171, wherein the pharmaceutically acceptable carrier is 0.9% saline. 173. The method of any one of claims 169–172, wherein the injectable composition comprises 2.0 mg/ml of the peptide or about 2.0 mg/ml. 174. The method of any one of claims 169–173, wherein the injectable composition comprises 50 mg/ml of the bulking agent or about 50 mg/ml of the bulking agent. 175. The method of any one of claims 169–174, wherein the injectable composition has a pH of from 2 to 4.5. 176. The method of claim 175, wherein the pH of the injectable composition is from 2.5 to 4. Attorney Docket No.55002-0003WO1 177. The method of claim 176, wherein the pH of the injectable composition is 3 or about 3. 178. An injectable composition produced according to the method of any one of claims 169–177. 179. Use of the lyophilized composition of any one of claims 1–25, 52–70 or 149– 156, or the lyophilized composition within the container of any one of claims 26–70; and/or a pharmaceutically acceptable carrier in the production of an injectable composition. 180. A kit comprising: the container of any one of claims 26–70 and a syringe. 181. The kit of claim 180, further comprising a reconstitution needle, optionally a 21 G x 1.5 in needle. 182. The kit of claim 180 or 181, further comprising an injection needle, optionally a 22 G x 7 in Quincke type point needle. 183. The kit of any one of claims 180–182, wherein the syringe is a 1, 2, 3, 4, or 5 cc syringe. 184. The kit of any one of claims 180–183, wherein the syringe is a 3 cc syringe. 185. The kit of any one of claims 180–184, further comprising instructions for administration. 186. A method comprising: administering the injectable composition of claim 178 to a patient. 187. A method of inhibiting TGF-ȕ1 in cell(s) of a patient, the method comprising: administering the injectable composition of claim 178 to the patient. 188. A method of treating a patient with a disease or disorder associated with overexpression of TGF-ȕ1, the method comprising: Attorney Docket No.55002-0003WO1 administering the injectable composition of claim 178 to the patient. 189. The method of any one of claims 186–188, wherein the composition is administered by injection, optionally intradiscal injection.