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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 26 Sept 2000

Boder E T, Midelfort K S, Wittrup K D

Abstract excerpt

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...

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Identifiers

PMID: 10984501
DOI: 10.1073/pnas.170297297
PMCID: PMC27086

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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