Structure-Based Design of Supercharged, Highly Thermoresistant Antibodies
Carolina Digital Repository (University of North Carolina at Chapel Hill)(2012)
摘要
Mutation of surface residues to charged amino acids increases resistance to aggregation and can enable reversible unfolding. We have developed a protocol using the Rosetta computational design package that “supercharges” proteins while considering the energetic implications of each mutation. Using a homology model, a single-chain variable fragment antibody was designed that has a markedly enhanced resistance to thermal inactivation and displays an unanticipated ≈30-fold improvement in affinity. Such supercharged antibodies should prove useful for assays in resource-limited settings and for developing reagents with improved shelf lives.
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关键词
Antibody Engineering,Protein Aggregation,Refolding
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