Hair Growth Peptide Stabilization in Topical Formulations

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.

Source

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.

Source

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.

Source

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.

Source

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.

Source

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.

Source

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.

Source

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.

Source

Formulations that enhance the stability, reduce aggregation, and immunogenicity of therapeutic peptides and proteins through the addition of surfactants, particularly alkylglycosides. The surfactants improve the formulation's performance in therapeutically relevant applications by preventing protein aggregation, enhancing bioavailability, and reducing immunogenic responses. The surfactants are particularly effective in formulations where protein aggregation is a critical issue, such as in peptide or protein therapeutics. The surfactants can be used alone or in combination with other stabilizing agents to achieve optimal performance in various formulations.

Source

Stabilizing deamidation-prone peptides and proteins against non-enzymatic degradation through the use of organic anions with pKa values between 0.5 and 3.5. The stabilizers combine with peptides or proteins in a molar excess to the number of susceptible asparaginyl or glutaminyl residues, effectively neutralizing the deamidation reaction mechanism. The stabilizers are particularly effective in aqueous solutions and can be used in formulations with minimal excipient amounts.

Source