Synthetic non-peptide mimetics of α-helices

Jessica M. Davis, Lun K. Tsou, Andrew Hamilton

Research output: Contribution to journalArticle

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 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 languageEnglish (US)
Pages (from-to)326-334
Number of pages9
JournalChemical Society Reviews
Volume36
Issue number2
DOIs
StatePublished - 2007

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Proteins
Molecules
Conformations
Membrane Proteins
RNA
DNA

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Synthetic non-peptide mimetics of α-helices. / Davis, Jessica M.; Tsou, Lun K.; Hamilton, Andrew.

In: Chemical Society Reviews, Vol. 36, No. 2, 2007, p. 326-334.

Research output: Contribution to journalArticle

Davis, Jessica M. ; Tsou, Lun K. ; Hamilton, Andrew. / Synthetic non-peptide mimetics of α-helices. In: Chemical Society Reviews. 2007 ; Vol. 36, No. 2. pp. 326-334.
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