Stability engineering of antibody single-chain Fv fragments

被引：479

作者：

Wörn, A ^{[1
]}

Plückthun, A ^{[1
]}

机构：

[1] Univ Zurich, Inst Biochem, CH-8057 Zurich, Switzerland

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2001年 / 305卷 / 05期

关键词：

protein stability; scFv fragments; recombinant antibodies; antibody engineering; protein folding;

D O I：

10.1006/jmbi.2000.4265

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The application of single-chain Fv fragments (scFv) in medicine and biotechnology places great demands on their stability. Only recently has attention been given to the production of highly stable scFvs, and in a number of examples it was found that such fragments indeed perform better during practical applications. The structural parameters influencing scFv stability are now beginning to be elucidated. This review summarizes progress in rational and evolutionary engineering methods, the structural implications of these results, as well as some examples where stability engineering has been successfully applied. (C) 2001 Academic Press.

引用

页码：989 / 1010

页数：22

共 139 条

[1] Factors influencing the dimer to monomer transition of an antibody single-chain Fv fragment [J].