α-Helix mimetics: Outwards and upwards

Madura K P Jayatunga, Sam Thompson, Andrew Hamilton

Research output: Contribution to journalArticle

Abstract

α-Helices are common secondary structural elements forming key parts of the large, generally featureless interfacial regions of many therapeutically-relevant protein-protein interactions (PPIs). The rational design of helix mimetics is an appealing small-molecule strategy for the mediation of aberrant PPIs, however the first generation of scaffolds presented a relatively small number of residues on a single recognition surface. Increasingly, helices involved in PPIs are found to have more complex binding modes, utilizing two or three recognition surfaces, or binding with extended points of contact. To address these unmet needs the design and synthesis of new generations of multi-sided, extended, and supersecondary structures are underway.

Original languageEnglish (US)
Pages (from-to)717-724
Number of pages8
JournalBioorganic and Medicinal Chemistry Letters
Volume24
Issue number3
DOIs
StatePublished - Feb 1 2014

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Proteins
Scaffolds
Molecules

Keywords

  • Peptidomimetic
  • Protein-protein interaction
  • Proteomimetic
  • Rational design

ASJC Scopus subject areas

  • Pharmaceutical Science
  • Drug Discovery
  • Organic Chemistry
  • Molecular Medicine
  • Molecular Biology
  • Clinical Biochemistry
  • Biochemistry

Cite this

α-Helix mimetics : Outwards and upwards. / Jayatunga, Madura K P; Thompson, Sam; Hamilton, Andrew.

In: Bioorganic and Medicinal Chemistry Letters, Vol. 24, No. 3, 01.02.2014, p. 717-724.

Research output: Contribution to journalArticle

Jayatunga, Madura K P ; Thompson, Sam ; Hamilton, Andrew. / α-Helix mimetics : Outwards and upwards. In: Bioorganic and Medicinal Chemistry Letters. 2014 ; Vol. 24, No. 3. pp. 717-724.
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