Hydrogen-bonded synthetic mimics of protein secondary structure as disruptors of protein-protein interactions

Marc J. Adler, Andrew G. Jamieson, Andrew Hamilton

Research output: Contribution to journalArticle

Abstract

Small molecules which can mimic the key structural facets of protein secondary structure, in particular the a-helix, b-strand, and b-sheet, have been shown to be potent disruptors of protein-protein interactions. Researchers have recently taken the organizational imitation of protein secondary structure to a new level by using intramolecular hydrogen bonds as stabilizing forces in these small molecule mimetics. The inclusion of these interactions invokes a conformational bias of the system, allowing for greater control of the appearance, and thus often function, of these molecules by design.

Original languageEnglish (US)
Pages (from-to)1-23
Number of pages23
JournalCurrent Topics in Microbiology and Immunology
Volume348
Issue number1
DOIs
StatePublished - 2010

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Secondary Protein Structure
Hydrogen
Proteins
Research Personnel

ASJC Scopus subject areas

  • Immunology and Allergy
  • Microbiology (medical)
  • Immunology
  • Microbiology

Cite this

Hydrogen-bonded synthetic mimics of protein secondary structure as disruptors of protein-protein interactions. / Adler, Marc J.; Jamieson, Andrew G.; Hamilton, Andrew.

In: Current Topics in Microbiology and Immunology, Vol. 348, No. 1, 2010, p. 1-23.

Research output: Contribution to journalArticle

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