Issue 2, 2007

Synthetic non-peptide mimetics of α-helices

Abstract

Proteins in nature fold into native conformations in which combinations of peripherally projected aliphatic, aromatic and ionic functionalities direct a wide range of properties. α-Helices, one of the most common protein secondary structures, serve as important recognition regions on protein surfaces for numerous proteinprotein, protein–DNA and protein–RNA interactions. These interactions are characterized by conserved structural features within the α-helical domain. Rational design of structural mimetics of these domains with synthetic small molecules has proven an effective means to modulate such protein functions. In this tutorial review we discuss strategies that utilize synthetic small-molecule antagonists to selectively target essential proteinprotein interactions involved in certain diseases. We also evaluate some of the proteinprotein interactions that have been or are potential targets for α-helix mimetics.

Graphical abstract: Synthetic non-peptide mimetics of α-helices

Article information

Article type
Tutorial Review
Submitted
11 Sep 2006
First published
04 Jan 2007

Chem. Soc. Rev., 2007,36, 326-334

Synthetic non-peptide mimetics of α-helices

J. M. Davis, L. K. Tsou and A. D. Hamilton, Chem. Soc. Rev., 2007, 36, 326 DOI: 10.1039/B608043J

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