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 protein–protein, 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 protein–protein interactions involved in certain diseases. We also evaluate some of the protein–protein interactions that have been or are potential targets for α-helix mimetics.
|Original language||English (US)|
|Number of pages||9|
|Journal||Chemical Society Reviews|
|State||Published - Jan 30 2007|
ASJC Scopus subject areas