Stapled peptides as potential therapeutics

McDougall, L. and Jamieson, A. G. (2019) Stapled peptides as potential therapeutics. In: Encyclopedia of Life Sciences. Wiley: Chichester. ISBN 9780470015902 (doi: 10.1002/9780470015902.a0028403)

Abstract

Stapled peptides are an important class of conformationally constrained, bioactive α‐helical peptides. They have been used extensively as chemical probes for the regulation of protein–protein interactions (PPIs), with one currently progressing through late‐stage clinical trials as a peptide drug candidate. Their ability to interact with shallow protein–protein interfaces, which have previously proven to be challenging to target with small molecules, has led to their rapid uptake by the chemical biology and drug discovery communities. Stapled peptides overcome some of the undesirable physicochemical properties that limit the use of peptides as therapeutics. They generally exhibit good binding affinity and specificity as they aim to accurately reproduce the α‐helix recognition motif from a PPI interface. They are protease resistant and in some instances have shown good cell permeability. The development of stapled peptides has thus resulted in a transformative shift by validating difficult PPIs as therapeutic targets and providing promising drug candidates.

• Item Type: Book Sections
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Jamieson, Professor Andrew and McDougall, Miss Laura
• Authors: McDougall, L., and Jamieson, A. G.
• College/School: College of Science and Engineering > School of Chemistry
• Journal Name: eLS
• Publisher: Wiley
• ISBN: 9780470015902