Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity

Boder ET.; Wittrupt KD.; Midelfort KS.

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Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity

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Single-chain antibody mutants have been evolved in vitro with antigen-binding equilibrium dissociation constant K-d = 48 fM and slower dissociation kinetics (half-time > 5 days) than those for the streptavidin-biotin complex. These mutants possess the highest monovalent ligand-binding affinity yet reported for an engineered protein by over two orders of magnitude. Optimal kinetic screening of randomly mutagenized libraries of 10(5)-10(7) yeast surface-displayed antibodies enabled a >1,000-fold decrease in the rate of dissociation after four cycles of affinity mutagenesis and screening. The consensus mutations are generally nonconservative by com parison with naturally occurring mouse Fv sequences and with residues that do not contact the fluorescein antigen in the wildtype complex. The existence of these mutants demonstrates that the antibody Fv architecture is not intrinsically responsible far an antigen-binding affinity ceiling during in vivo affinity maturation. References: 48

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《Proceedings of the National Academy of Sciences of the United States of America》 |2000年第20期|10701-10705|共5页
作者
Boder ET.; Wittrupt KD.; Midelfort KS.;
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作者单位

Univ Illinois, Dept Chem Engn, Urbana, IL 61801, USA, .;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
Yeast surface display; In-vitro; Polypeptide libraries; Fluorescyl antibodies; Molecular-dynamics; Ligand-binding; Phage display; Selection; Protein; Maturation;

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机译：Expression of actively soluble antigen-binding fragment (Fab) antibody and GFP fused Fab in the cytoplasm of the engineered Escherichia coli
2. Fluorescence-labelled antigen-binding fragments (Fab) from monoclonal antibody 5F12 detect human erythropoietin in immunoaffinity capillary electrophoresis [J] . Claus Bornemann, Tilman Burggraef, Gunter HeimbuchelFranz-Georg HanischSandra Winkels Analytical and bioanalytical chemistry . 2003,第7期

机译：Fluorescence-labelled antigen-binding fragments (Fab) from monoclonal antibody 5F12 detect human erythropoietin in immunoaffinity capillary electrophoresis
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机译：Targeted therapy by gene transfer of a monovalent antibody fragment against the Met oncogenic receptor

Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity

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