Abstract
Since the emergence of recombinant DNA technology from the lab to commercialization, biotechnology protein drugs have garnered an increased share of new molecular entities (NMEs) in development pipelines (Mullin 2004). Monoclonal antibodies have rapidly become one of the major shares of this market with about 25% of biotech products in development. As with any other protein pharmaceutical monoclonal antibodies can degrade both by chemical and physical pathways. One of the most important pathways for protein physical degradation is the generation of protein aggregates. The ability of proteins to aggregate has been recognized from the early beginnings in protein biochemistry, and has become an important degradation pathway that can have a major impact on the safety and efficacy of protein drugs.
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Andya, J.D., Liu, J., Shire, S.J. (2010). Analysis of Irreversible Aggregation, Reversible Self-association and Fragmentation of Monoclonal Antibodies by Analytical Ultracentrifugation. In: Shire, S., Gombotz, W., Bechtold-Peters, K., Andya, J. (eds) Current Trends in Monoclonal Antibody Development and Manufacturing. Biotechnology: Pharmaceutical Aspects, vol XI. Springer, New York, NY. https://doi.org/10.1007/978-0-387-76643-0_13
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