Journal Article

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 and Kouhei Tsumoto

in The Journal of Biochemistry

Volume 162, issue 4, pages 255-258
Published in print October 2017 | ISSN: 0021-924X
Published online August 2017 | e-ISSN: 1756-2651 | DOI: https://dx.doi.org/10.1093/jb/mvx050
Thermodynamic analyses of amino acid residues at the interface of an antibody B2212A and its antigen roundabout homolog 1

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Abstract

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.

Keywords: affinity; antibody; interaction kinetics; mutation analysis; thermal stability

Journal Article.  2303 words.  Illustrated.

Subjects: Cell Biology ; Biotechnology ; Biochemistry ; Molecular and Cell Biology

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