Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation |
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Authors: | Chi Eva Y. Krishnan Sampathkumar Randolph Theodore W. Carpenter John F. |
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Affiliation: | (1) Department of Chemical Engineering, Center for Pharmaceutical Biotechnology, ECCH 111, University of Colorado, Campus Box 424, Boulder, Colorado;(2) Department of Pharmaceutics and Drug Delivery, Amgen Inc., Thousand Oaks, California;(3) Department of Pharmaceutical Sciences, School of Pharmacy, University of Colorado Health Sciences Center, Denver, Colorado |
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Abstract: | Irreversible protein aggregation is problematic in the biotechnology industry, where aggregation is encountered throughout the lifetime of a therapeutic protein, including during refolding, purification, sterilization, shipping, and storage processes. The purpose of the current review is to provide a fundamental understanding of the mechanisms by which proteins aggregate and by which varying solution conditions, such as temperature, pH, salt type, salt concentration, cosolutes, preservatives, and surfactants, affect this process. |
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Keywords: | formulation pharmaceuticals denaturation second virial coefficient conformational stability |
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