PMID: 12758084May 22, 2003Paper

Searching sequence space for high-affinity binding peptides using ribosome display

Journal of Molecular Biology
T Lamla, Volker A Erdmann

Abstract

We present the construction of a synthetic library based on the scaffold of bovine heart fatty acid-binding protein (FABP) with 1.1x10(14) independent members. Ribosome display was applied to select streptavidin-binding peptides in vitro from 2x10(13) molecules of the library each encoding FABP with 15 contiguous random amino acid residues at its N terminus. The selection yielded several different binding peptides. The best binder possessed a dissociation constant as low as 4nM and, in contrast to the previously isolated peptides, contained no HPQ motif. A substitution analysis enabled shortening of the 15-mer peptide and revealed a 9-mer variant with a dissociation constant of 17nM, which is a 1000-fold increase of affinity compared to the already known peptides of this size. This high-affinity binding peptide in combination with the whole set of streptavidin conjugates should be an extremely useful tool for the detection and purification of recombinant proteins.

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Citations

Nov 19, 2004·Journal of Molecular Recognition : JMR·Rebecca L Rich, David G Myszka
Feb 23, 2010·Amino Acids·Zheng MiaoZhen Cheng
Dec 19, 2003·Protein Expression and Purification·Thorsten Lamla, Volker A Erdmann
Oct 9, 2007·Journal of the American Chemical Society·S Jarrett WrennPehr B Harbury
Mar 1, 2007·Nature Methods·Christian ZahndAndreas Plückthun
Nov 8, 2008·Protein Engineering, Design & Selection : PEDS·G A KuzmichevaV A Petrenko
May 19, 2010·Antimicrobial Agents and Chemotherapy·Fang ChenXiao-Lian Zhang
Jun 30, 2009·BMC Biotechnology·Yiran Wang, Y-H Percival Zhang
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Aug 6, 2004·Protein Expression and Purification·Michael D ScholleBrian K Kay
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Aug 14, 2020·ACS Combinatorial Science·Kaitlyn BaconStefano Menegatti
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Oct 22, 2021·FEMS Microbiology Reviews·Weronika JaroszewiczGrzegorz Węgrzyn

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