Disrupting protein-protein interactions with non-peptidic, small molecule α-helix mimetics

Christopher G. Cummings, Andrew D. Hamilton

Research output: Contribution to journalReview articlepeer-review

Abstract

Many biological processes are regulated by protein-protein interactions (PPIs) and as such their misregulation can cause a multitude of diseases. Often the interactions between large proteins are mediated by small protein secondary structural domains, which project a minimum number of specifically arranged residues into the complementary surface of an interacting protein. Nature has the advantage of time, and over time has optimized those secondary structures, such as α-helices, β-sheets and β-strands, found at the interfaces of PPIs. Inspired by Nature's extensive optimization, chemists have used these secondary structures as templates in the design of small molecules that may act as structural and functional mimics of large rhenylogically organized protein secondary structures. Herein recent applications of the indane, terphenyl, terphenyl-inspired templates, polycyclic ether and benzodiazepinedione scaffolds, as non-peptidic, small molecule α-helix mimetics, to disrupt PPIs are detailed.

Original languageEnglish (US)
Pages (from-to)341-346
Number of pages6
JournalCurrent Opinion in Chemical Biology
Volume14
Issue number3
DOIs
StatePublished - Jun 2010

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry

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