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• W2130542921 abstract "Therapeutic proteins are exposed to various wetted surfaces that could shed subvisible particles. In this work we measured the adsorption of a monoclonal antibody (mAb) to various microparticles, characterized the adsorbed mAb secondary structure, and determined the reversibility of adsorption. We also developed and used a front-face fluorescence quenching method to determine that the mAb tertiary structure was near-native when adsorbed to glass, cellulose, and silica. Initial adsorption to each of the materials tested was rapid. During incubation studies, exposure to the air–water interface was a significant cause of aggregation but acted independently of the effects of microparticles. Incubations with glass, cellulose, stainless steel, or Fe2O3 microparticles gave very different results. Cellulose preferentially adsorbed aggregates from solution. Glass and Fe2O3 adsorbed the mAb but did not cause aggregation. Adsorption to stainless steel microparticles was irreversible, and caused appearance of soluble aggregates upon incubation. The secondary structure of mAb adsorbed to glass and cellulose was near-native. We suggest that the protocol described in this work could be a useful preformulation stress screening tool to determine the sensitivity of a therapeutic protein to exposure to common surfaces encountered during processing and storage. © 2009 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 98:3218–3238, 2009" @default.
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• W2130542921 date "2009-09-01" @default.
• W2130542921 modified "2023-10-02" @default.
• W2130542921 title "Monoclonal antibody interactions with micro- and nanoparticles: Adsorption, aggregation, and accelerated stress studies" @default.
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• W2130542921 doi "https://doi.org/10.1002/jps.21768" @default.
• W2130542921 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2749556" @default.
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