Therapeutic proteins such as monoclonal antibodies are commonly subjected to freeze-thawing for analytical testing, shipping, and storage. Freeze-thawing stress can potentially expose protein molecules to the ice-liquid interface and induce degradation through protein aggregation. We studied the effects of freeze-thawing on aggregation of an IgG<sub>2</sub> monoclonal antibody, specifically during Protein A purification. Several solution conditions including pH and protein concentration were found to significantly impact aggregation of the antibody during freeze-thawing. Based on these findings, the proposed mitigation strategy aims to minimize freeze-thaw related aggregation during small-scale process development, analytical testing, and manufacturing. In addition, the process parameters of the Protein A chromatography step were modified to further reduce aggregate levels.

Effect of freeze-thaw, protein concentration, and pH on antibody aggregation in bioprocess protein A chromatography

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.