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Issue 9, 2011
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A novel β-loop scaffold of phage-displayed peptides for highly specific affinities

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Abstract

Loop peptides stabilized by two β-strands were used as a scaffold for a phage displayed peptide library. Affinity-based screening for insulin provided peptides, which showed affinity constants of 105 M−1 order for insulin over 100 times greater than their affinity for the structurally similar insulin-like growth factor 1. The results suggested that the scaffold offers a powerful tool for generating and screening peptides as ligands for drugs and biologics.

Graphical abstract: A novel β-loop scaffold of phage-displayed peptides for highly specific affinities

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Supplementary files

Article information


Submitted
01 Mar 2011
Accepted
25 May 2011
First published
08 Jun 2011

Mol. BioSyst., 2011,7, 2558-2562
Article type
Communication

A novel β-loop scaffold of phage-displayed peptides for highly specific affinities

T. Sawada, K. Ishiguro, T. Takahashi and H. Mihara, Mol. BioSyst., 2011, 7, 2558
DOI: 10.1039/C1MB05085K

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