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Article

Directed in vitro evolution and crystallographic analysis of a peptide-binding single chain antibody fragment (scFv) with low picomolar affinity.

The Journal of biological chemistry - 30 Apr 2004

Zahnd Christian, Spinelli Silvia, Luginbühl Béatrice, Amstutz Patrick, Cambillau Christian, Plückthun Andreas

Abstract excerpt

We generated a single chain Fv fragment of an antibody (scFv) with a binding affinity of about 5 pm to a short peptide by applying rigorous directed evolution. Starting from a high affinity peptide binder, originally obtained by ribosome display from a murine library, we generated libraries of mutants with error-prone PCR and DNA shuffling and applied off-rate selection by using ribosome display. Crystallographic...

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Identifiers

PMID: 14754898
DOI: 10.1074/jbc.M309169200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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