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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Chi, E.Y., Krishnan, S., Randolph, T.W. et al. Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation. Pharm Res 20, 1325–1336 (2003). https://doi.org/10.1023/A:1025771421906
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DOI: https://doi.org/10.1023/A:1025771421906