Protein & peptide formulation
Given the instable nature of proteins and peptides, optimizing the stability of such therapeutics is a critical yet challenging objective of any drug development program. Resolution of such challenges enables their full therapeutic potential to be exploited, thereby ensuring optimal treatment options.
Safety and activity can be impaired by loss of “integrity” of the formulated product. Proteins and peptides indeed are only marginally stable and can undergo degradation via several mechanisms:
- Hydrophobic interactions and peptide fibrillation may lead to aggregates and sub-visible particles, resulting in reduced efficacy and increased immunogenicity.
- Binding to surfaces can cause structural changes resulting in self-association and/or aggregation. Further to this, non-specific adsorption to drug containers may cause material loss and incorrect dosing.
- Chemical stress, such as degradation by oxidative species, can result in a range of functional changes such as altered binding activities, increased susceptibility to aggregation and proteolysis, and increased or decreased uptake by cells, as well as altered immunogenicity.
Choosing the right formulation strategy
Companies often work within a standard toolbox of excipients for formulation development. Although many of these agents are effective stabilizers, their use requires careful consideration in terms of local toxicity and potential immunogenicity. Often the outcome is a cocktail of excipients. In some instances, it is quite difficult to combine the various “ingredients” to reach the levels of stabilization needed. As formulation becomes increasingly complicated to achieve, there is an equally increased need for advanced solutions.
Albumin is nature’s own stabilizer, with in vivo functions to transport and protect vital molecules. Our recombinant human albumin, Recombumin® exploits albumin’s multifunctional properties as an effective, versatile stabilizer. It is particularly suited as a leaner formulation approach of biological drugs, such as proteins or peptides, not readily stabilized using traditional formulation strategies.