Interactions and Phase Behavior of a Monoclonal Antibody
Interactions and Phase Behavior of a Monoclonal Antibody
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DOI：
10.1002/btpr.536
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发表时间：
2011-01-01
影响因子：
2.9
通讯作者：
Sandler, Stanley I.
中科院分区：
文献类型：
--
作者：
Lewus, Rachael A.;Darcy, Patricia A.;Sandler, Stanley I.
Protein phase behavior is implicated in numerous aspects of downstream processing either by design, as in crystallization or precipitation processes, or as an undesired effect, such as aggregation. An improved understanding of protein phase behavior is, therefore, important for developing rational design strategies for important process steps. This work explores the phase behavior of a monoclonal antibody (mAb), IDEC-152, which exhibits liquid-liquid separation, aggregation, gelation, and crystallization. A systematic study of numerous factors, including the effects of solution composition and pH, has been conducted to explore the phase behavior of this antibody. Phenomena observed include a significant dependence of the cloud point on the cation in sulfate salts and nonmonotonic trends in pH dependence. Additionally, conditions for crystallization of this mAb are reported for the first time. Protein-protein interactions, as determined from the osmotic second virial coefficient, are used to interpret the phase behavior. (C) 2011 American Institute of Chemical Engineers Biotechnol. Prog., 27: 280-289, 2011
