Regulation of protein–protein interactions using stapled peptides

Jamieson, A. and Robertson, N. (2015) Regulation of protein–protein interactions using stapled peptides. Reports in Organic Chemistry, 2015(5), pp. 65-74. (doi: 10.2147/ROC.S68161)

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The targeting of protein–protein interactions (PPIs) that include secondary structure motifs such as the α-helix and ß-sheet is a challenge in chemical biology. A new class of compounds called stapled peptides have been developed that mimic α-helix secondary structures involved in PPIs. These conformationally constrained peptides also show favorable physicochemical properties and so are promising lead compounds for drug discovery. This review focuses on the design aspects of hydrocarbon constrained α-helical proteomimetics and provides examples in which they target biologically relevant PPIs.

Item Type:Articles
Additional Information:The authors thank the Engineering and Physical Sciences Research Council (EPSRC) (EP/L018152/1) and University of Leicester for financial support.
Glasgow Author(s) Enlighten ID:Jamieson, Professor Andrew
Authors: Jamieson, A., and Robertson, N.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Reports in Organic Chemistry
Publisher:Dove Medical Press
Copyright Holders:Copyright © 2015 Robertson and Jamieson
First Published:First published in Reports in Organic Chemistry 2015(5):64-74
Publisher Policy:Reproduced under a Creative Commons License

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