ArticlePharmaceutical research2024
Stress-mediated polysorbate 20 degradation and its potential impact on therapeutic proteins.
Article in Pharmaceutical research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- Phosphatidylcholine-Polysorbate 20-Based Mixed Micelles: A New Option to Prevent Protein Aggregation?Pharmaceutics · 2026Article
- Formulation of Recombinant Therapeutic Proteins: Technological Innovation, Regulations, and Evolution Towards Buffer-Free Formulations.Pharmaceutics · 2025Review
- Reduced IgG1 Antibody Left-Twisted Antiparallel β-Sheet Structure Stability Occurs under Metal-Catalyzed Oxidation Conditions in the Presence of Polysorbates.Molecular pharmaceutics · 2025Article
- Polysorbates degrading enzymes in biotherapeutics - a current status and future perspectives.Frontiers in bioengineering and biotechnology · 2024Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposePolysorbates are the most commonly used surfactants in formulations to stabilize therapeutic proteins against interfacial stresses. Polysorbates can undergo oxidative or enzyme-mediated hydrolytic degradation to produce free fatty acids (FFAs) and subvisible particles in formulations. To determine which product related variables contribute to PS20 degradation, we investigated the effects of storage temperature, formulation, pH, presence of hydrolytic enzymes, and specific fatty acid composition on different grades of PS20 in relation to their PS20 degradation profile and consequently the quality of protein drug products.
methodsBevacizumab and T-DM1 were reformulated in the freshly prepared therapeutic protein formulations containing either compendial PS20 or non-compendial PS20 with high % lauric acid and spiked with exogenous esterase or lipase. The release of FFAs and formation of particles were monitored at 4°C and 37°C. Protein quality was assessed for secondary structures, purity, and biological activity.
resultsHydrolytic release of FFAs and formation of subvisible particles were found to be dependent on grades of PS20, types of enzymes used, incubation temperature, and pH. Esterase- or lipase-mediated degradation of PS20 and formation of subvisible particles in drug formulation showed no significant impact on the biological activity and stability of therapeutic proteins against degradation or aggregation.
conclusionsOur study suggests that degradation of PS20 and formation of FFA particles depend on the fatty acid composition of PS20, types of hydrolytic enzymes, pH, and temperature. The presence of FFA subvisible particles showed no significant impact on the purity and biological activity of the therapeutic proteins under the tested conditions.
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