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. 1993 Aug 1;293(Pt 3):613–616. doi: 10.1042/bj2930613

Biotin binders selected from a random peptide library expressed on phage.

I Saggio 1, R Laufer 1
PMCID: PMC1134410  PMID: 8352728

Abstract

Recombinant biotin-binding phages were affinity-selected from a random peptide library expressed on the surface of filamentous phage. Phage binding to biotinylated proteins was half-maximally inhibited by micromolar concentrations of a monobiotinylated molecule. Sequencing of the peptide inserts of selected phages led to the identification of a previously unknown biotin-binding motif, CXWXPPF(K or R)XXC. A synthetic peptide containing this sequence motif inhibited streptavidin binding to biotinylated BSA with an IC50 of 50 microM. This compound represents the shortest non-avidin biotin-binding peptide identified to date. Our results illustrate that phage display technology can be used to identify novel ligands for a small non-proteinaceous molecule.

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Selected References

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