Hair Growth Peptide Stabilization in Topical Formulations

A stable pharmaceutical composition for treating hypertension containing midkine analogue natriuretic peptide (MANP), acetate, sucrose, and polysorbate 20. The composition has a specific concentration range for MANP, acetate, sucrose, and polysorbate 20, and a pH and osmolality within certain ranges. This formulation provides long-term stability of MANP for 24 months at 5°C without significant degradation or aggregation.

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Composition and method for inhibiting protein aggregation through the use of acetyl-L-arginine, a naturally occurring amino acid. The composition, comprising acetyl-L-arginine or its salt, effectively suppresses protein aggregation by modulating protein conformation and interactions. This therapeutic agent can be used to prevent protein aggregation in therapeutic proteins, vaccines, and biologic formulations, thereby maintaining their stability and preventing adverse effects.

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Hydroxypropyl methylcellulose acetate succinate (HPMCAS) derivatives as polymeric excipients for stabilizing proteins in spray dried formulations, particularly in high-temperature processing and low-pH environments. The HPMCAS derivatives provide protection against protein degradation through both heat-stabilization and pH-neutralization mechanisms, while maintaining the protein's native conformation. The formulation can be used to prepare stable, biologically active proteins for spray drying applications, including antibodies, peptides, and proteins in drug formulations.

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Stable liquid formulations of therapeutic fusion proteins, particularly CTLA-4-Ig, comprising histidine buffer, amino acid, stabilizer, and surfactant, which achieve optimal protein concentration, low viscosity, and reduced aggregation. The formulations incorporate a buffer system optimized for fusion protein stability, combined with specific amino acids and surfactants to prevent protein aggregation and maintain therapeutic activity. The formulations are suitable for clinical applications requiring high protein concentrations, particularly in autoimmune diseases like rheumatoid arthritis and psoriasis.

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A pharmaceutical composition that stabilizes peptides in the gastrointestinal tract, particularly in the colon, through the synergistic action of amino acids and dipeptides. The composition comprises a peptide as the active ingredient, combined with one or more amino acids, dipeptides, or a combination thereof. This combination enables the peptide to maintain its biological activity while protecting it from degradation in the colon environment, making it suitable for rectal administration.

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A method for reducing protein viscosity in formulations through the addition of camphorsulfonic acid as an excipient, specifically at concentrations where it exhibits a viscosity-reducing effect. The method enables the creation of stable protein solutions at concentrations typically associated with subcutaneous administration, while maintaining protein stability and preventing aggregation. The camphorsulfonic acid excipient selectively lowers protein viscosity without compromising protein structure, making it an effective solution for protein formulations requiring low-volume delivery.

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A novel glucagon formulation that enhances its stability and solubility at physiological pH, enabling effective treatment of hypoglycemia. The formulation comprises a modified glucagon molecule with a chemically active prodrug moiety that is cleaved in vivo to release the active glucagon. The prodrug moiety contains a phosphorylated amino acid residue that prevents amyloid β-fibril formation and maintains glucagon's solubility at neutral pH. This approach addresses the traditional challenges of glucagon formulation, including its poor solubility and instability at physiological pH, while preserving its biological activity.

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Pharmaceutical compositions containing peptides, their derivatives, or their analogs, or their salts and co-crystals, that retain at least 80% of the potency of the active ingredient after storage at room temperature for at least four months. The compositions can be prepared using a pharmaceutically acceptable carrier that maintains the active ingredient's potency during storage.

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Aqueous solution compositions of therapeutic agents, particularly peptides, at low buffer concentrations that maintain stability through minimal buffering requirements. The compositions contain a peptide therapeutic agent with no or very low ionisable groups with pKa in the range 3.0-8.5, and a stabilizer that maintains a buffer concentration of 0-5 mM. This composition approach enables peptide therapeutics to maintain their biological activity at elevated temperatures without degradation, while maintaining pH stability.

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A lyophilized pharmaceutical composition comprising a Fc-peptide fusion protein, buffer, bulking agent, stabilizer, and surfactant that maintains therapeutic activity and stability over extended periods. The formulation is designed to prevent protein denaturation and aggregation, ensuring sustained bioavailability of the therapeutic agent. The composition maintains optimal pH and buffer conditions between 4.0 and 6.0, with specific buffer and bulking agent concentrations optimized for the fusion protein. The surfactant component prevents protein adsorption, while the stabilizer maintains protein integrity. The formulation provides a stable lyophilized product suitable for therapeutic use with high protein concentration.

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Polypeptides for treating dry eye disease that maintain their therapeutic activity through reduced degradation. The compositions contain a specific peptide sequence that is highly resistant to degradation, with minimal degradation products detected in formulations that contain less than 5% degradation products. The peptide maintains its therapeutic efficacy through specific structural features that prevent hydrolysis and aggregation. The compositions can be administered topically or as liquid eye drops and exhibit sustained therapeutic activity over extended periods.

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Stable pharmaceutical formulations containing anti-myostatin adnectins that inhibit myostatin activity and signaling. The adnectins are derived from fibronectin and contain a fibronectin type III domain (Fn3) fragment. They can be administered subcutaneously to treat muscle wasting disorders, metabolic disorders, and bone degenerative conditions through a single injection. The formulations exhibit improved stability compared to traditional protein formulations that require multiple excipients to prevent aggregation.

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A pharmaceutical composition comprising neo-antigenic peptides, a pH modifier present at a concentration of less than 1.0 mM, and a pharmaceutically acceptable carrier. The composition enables the use of previously insoluble neo-antigenic peptides in pharmaceutical formulations by lowering the pH to solubility threshold levels. This composition can be used to develop personalized cancer vaccines and immunogenic compositions that overcome common challenges in neoantigen delivery, including poor solubility and immunogenicity issues.

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Magnesium-stabilized aqueous pharmaceutical formulations of etanercept that maintain stability during long-term storage. The formulations contain etanercept and a stabilizer containing 2-10 mM magnesium, which prevents aggregation, misfolding, and fragmentation of the protein. The stabilization mechanism involves magnesium binding to the native conformation of the etanercept protein, maintaining its native structure even after storage at 5°C for up to three months. The formulations exhibit superior thermal stability compared to existing formulations containing arginine, with HIC analysis showing less than 3% aggregate formation and less than 20% fragment content.

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Composition of free thiols and methods of making and using such compositions for enhanced protein stability. The compositions contain proteins with intact free thiol groups, which are crucial for maintaining protein structure and function under physiological conditions. The compositions achieve this stability through specific modifications, including the use of cysteine, cysteine hydrochloride, and methionine, and controlled levels of sugar and surfactants. The compositions are particularly useful for maintaining protein activity in aqueous solutions, particularly for proteins with disulfide bonds, and can be used as formulations for injectable solutions, sterile aqueous solutions, and lyophilized preparations.

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Pharmaceutical formulations that contain high concentrations of protein biomolecules, particularly for therapeutic applications, and incorporate amino acid stabilizers. The formulations achieve improved reconstitution times and stability compared to traditional formulations lacking stabilizers. The stabilizers are derived from amino acids like arginine, alanine, glycine, lysine, or proline, and are present in concentrations typically between 2-5% w/v. These stabilizers enhance protein stability without the need for sugar stabilizers, particularly beneficial for high-concentration protein formulations. The formulations can be packaged in lyophilized form for reconstitution, with the stabilizers incorporated into the lyophilized product.

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A peptide formulation that maintains stability and solubility in water through controlled pH and oxygen levels. The formulation comprises peptides stabilized by sucrose and sodium chloride, which are combined with a pH-controlled solution. The solution maintains optimal pH conditions (20-25°C) to prevent peptide degradation while maintaining solubility. This formulation enables stable peptide delivery in aqueous environments, particularly for peptides with critical stability requirements, such as the peptide sequence 3.

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Stabilized formulations containing a peptide, such as a glucagon, or a combination of peptides that exhibit little or no chemical degradation and/or aggregation of the peptide over an extended period of time. The formulations are in the form of a solution or suspension, which contain a solvent like glycerin, a thermal stabilizing excipient like a di-arginine piperazine, a pH-adjusting agent like sodium bicarbonate, a sugar like sucrose, and an antimicrobial agent like m-cresol.

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Stable protein formulations for injectable drugs that can be used at high concentrations without aggregation or precipitation. The formulations contain amino acids in addition to the protein to enhance stability and reduce viscosity. The amino acids can be different from each other and can be selected based on properties like charge, hydrophobicity, or polarity. This allows tuning of stability and viscosity independently. The formulations are suitable for injectable drugs like antibodies that are difficult to formulate at high concentrations due to instability.

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Peptide compositions that maintain transparency and mechanical stability during storage, particularly in peptide-based materials with self-assembling properties. The compositions contain a self-assembling peptide with a basic C-terminal residue, a buffer with a pKa of 3.5 or more and less than 7.5 containing nitrogen atoms, and water. The buffer maintains positive charge balance at the peptide composition's pH, preventing aggregation and maintaining transparency. The composition also exhibits excellent mechanical stability, making it suitable for applications requiring these properties.

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