Thermodynamic analyses of amino acid residues at the interface of an antibody B2212A and its antigen roundabout homolog 1.

Anna Yui, Hiroki Akiba, Shota Kudo, Makoto Nakakido, Satoru Nagatoishi, Kouhei Tsumoto

Journal of biochemistry 2017 Oct 01

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Artificial affinity maturation of antibodies is promising but often shows difficulties because the roles of each amino acid residue are not well known. To elucidate their roles in affinity against the antigen and thermal stability, interface residues in single-chain Fv of an antibody B2212A with its antigen roundabout homolog 1 were mutated and analyzed. Some amino acids played important roles in the affinity while others contributed to thermal stability. © The Authors 2017. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Citation

Anna Yui, Hiroki Akiba, Shota Kudo, Makoto Nakakido, Satoru Nagatoishi, Kouhei Tsumoto. Thermodynamic analyses of amino acid residues at the interface of an antibody B2212A and its antigen roundabout homolog 1. Journal of biochemistry. 2017 Oct 01;162(4):255-258