## Abstract Stainless steel is a ubiquitous surface in therapeutic protein production equipment and is also present as the needle in preβfilled syringe biopharmaceutical products. Stainless steel microparticles can cause the aggregation of a monoclonal antibody (mAb). The initial rate of mAb aggreg
Adsorption of monoclonal antibodies to glass microparticles
β Scribed by Matthew Hoehne; Fauna Samuel; Aichun Dong; Christine Wurth; Hanns-Christian Mahler; John F. Carpenter; Theodore W. Randolph
- Publisher
- John Wiley and Sons
- Year
- 2011
- Tongue
- English
- Weight
- 311 KB
- Volume
- 100
- Category
- Article
- ISSN
- 0022-3549
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β¦ Synopsis
Microparticulate glass represents a potential contamination to protein formulations that may occur as a result of processing conditions or glass types. The effect of added microparticulate glass to formulations of three humanized antibodies was tested. Under the three formulation conditions tested, all three antibodies adsorbed irreversibly at near monolayer surface coverages to the glass microparticles. Analysis of the secondary structure of the adsorbed antibodies by infrared spectroscopy reveal only minor perturbations as a result of adsorption. Likewise, front-face fluorescence quenching measurements reflected minimal tertiary structural changes upon adsorption. In contrast to the minimal effects on protein structure, adsorption of protein to suspensions of glass microparticles induced significant colloidal destabilization and flocculation of the suspension.
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A chromatographic method was employed to study the kinetics of human serum albumin (HSA) adsorbed on immobilized monoclonal antibodies. The antibodies of various specificities were covalently bound to a high-performance liquid chromatography (HPLC) silica support. For very low desorption rates, succ