How enzymatic hydrolysis of polysorbate 20 influences colloidal protein stability
European Journal of Pharmaceutical Sciences, ISSN: 0928-0987, Vol: 191, Page: 106597
2023
- 2Citations
- 10Captures
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Article Description
Polysorbates (PS) are esters of ethoxylated sorbitol anhydrides of different composition and are widely used surfactants in biologics. PSs are applied to increase protein stability and concomitant shelf-life via shielding against e.g., interfacial stresses. Due to the presence of specific lipolytic host cell protein (HCP) contaminations in the drug substance, PSs can be degraded via enzymatic hydrolysis. Surfactant hydrolysis leads to the formation of degradants, such as free fatty acids that might form fatty acid particles. In addition, PS degradation may reduce surfactant functionality and thus reduce the protection of the active pharmaceutical ingredient (API). Although enzymatic degradation was observed and reported in the last years, less is known about the relationship between certain polysorbate degradation patterns and the increase of mechanical and interfacial stress towards the API. In this study, the impact of specifically hydrolyzed polysorbate 20 (PS20) towards the stabilization of two monoclonal antibodies (mAbs) during accelerated shaking stress conditions was investigated. The results show that a specific enzymatic degradation pattern of PS20 can influence the colloidal stability of biopharmaceutical formulations. Furthermore, the kinetics of the appearance of visual phenomena, opalescence, and particle formation depended on the polysorbate degradation fingerprint as induced via the presence of surrogate enzymes. The current case study shows the importance of focusing on specific polysorbate ester fractions to understand the overall colloidal protein stabilizing effect. The performed study gives first insight into the functional properties of PS and helps to evaluate the impact of PS degradation in the formulation development of biopharmaceuticals in general.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0928098723002270; http://dx.doi.org/10.1016/j.ejps.2023.106597; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85173816784&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/37770006; https://linkinghub.elsevier.com/retrieve/pii/S0928098723002270; https://dx.doi.org/10.1016/j.ejps.2023.106597
Elsevier BV
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