Jump to main content
Jump to site search
Access to RSC content Close the message box

Continue to access RSC content when you are not at your institution. Follow our step-by-step guide.


Issue 12, 2009
Previous Article Next Article

Inhibition of protein–protein interactions using designed molecules

Author affiliations

Abstract

Although many cellular processes depend upon enzymatic reactions, proteinprotein interactions (PPIs) mediate a large number of important regulatory pathways and thus play a central role in disease development. In order to understand and selectively inhibit cellular signalling pathways, there is a pressing need for small molecules that target PPIs, particularly in the context of pharmaceutical development. This tutorial review will introduce the relevance of PPIs to chemical biology and highlight the key challenges in designing inhibitors. Some of the successes using conventional approaches to the identification of small-molecule PPI inhibitors will be highlighted, and also the reasons why these approaches have not always proven successful. Several general approaches tailored to particular protein topologies are emerging for the design of scaffolds that inhibit PPIs—these will form the major content of this review. Finally a summary of the challenges to be faced in developing inhibitors of PPIs into drug leads and how these challenges may differ from those encountered with enzyme-like targets will be given.

Graphical abstract: Inhibition of protein–protein interactions using designed molecules

Back to tab navigation

Article information


Submitted
30 Apr 2009
First published
27 Jul 2009

Chem. Soc. Rev., 2009,38, 3289-3300
Article type
Tutorial Review

Inhibition of proteinprotein interactions using designed molecules

A. J. Wilson, Chem. Soc. Rev., 2009, 38, 3289
DOI: 10.1039/B807197G

Social activity

Search articles by author

Spotlight

Advertisements