抗体B2212A与其抗原环化同源物1界面处氨基酸残基的热力学分析。

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

作者信息

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

机构信息

Department of Bioengineering, School of Engineering, The University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.

Laboratory of Pharmacokinetic Optimization, Center for Drug Design Research, National Institutes of Biomedical Innovation, Health and Nutrition, 7-6-8 Saito-Asagi, Ibaraki City, Osaka 567-0085, Japan.

出版信息

J Biochem. 2017 Oct 1;162(4):255-258. doi: 10.1093/jb/mvx050.

DOI:10.1093/jb/mvx050

PMID:28981752

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.

摘要

抗体的人工亲和力成熟很有前景，但往往存在困难，因为每个氨基酸残基的作用尚不清楚。为了阐明它们在对抗抗原的亲和力和热稳定性方面的作用，对抗体B2212A的单链Fv与其抗原迂回同源物1之间的界面残基进行了突变和分析。一些氨基酸在亲和力方面起重要作用，而另一些则有助于热稳定性。