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Interactions and phase behavior of a monoclonal antibody
Author(s) -
Lewus Rachael A.,
Darcy Patricia A.,
Lenhoff Abraham M.,
Sandler Stanley I.
Publication year - 2011
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1002/btpr.536
Subject(s) - crystallization , virial coefficient , phase (matter) , monoclonal antibody , precipitation , chemistry , protein aggregation , chemical physics , chemical engineering , chromatography , thermodynamics , antibody , biochemistry , physics , biology , organic chemistry , immunology , meteorology , engineering
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. © 2011 American Institute of Chemical Engineers Biotechnol. Prog., 2011