Ontology highlight
ABSTRACT:
SUBMITTER: Boder ET
PROVIDER: S-EPMC27086 | biostudies-literature | 2000 Sep
REPOSITORIES: biostudies-literature
Boder E T ET Midelfort K S KS Wittrup K D KD
Proceedings of the National Academy of Sciences of the United States of America 20000901 20
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 ...[more]