Hydrophobic side-chain interactions in a family of dimeric amide foldamers-potential alpha-helix mimetics

Oleg V. Kulikov, Christopher Incarvito, Andrew D. Hamilton

Research output: Contribution to journalArticle

Abstract

A series of new alpha-helix mimetics based on a benzamide scaffold and potentially able to disrupt protein-protein interactions have been synthesized and characterized by X-ray analysis. Inspection of the solid state structures of aromatic amide dimers confirmed that the molecules adopt a curved conformation with intramolecular H-bonding between the amide NH and the alkoxy oxygen of the neighboring aromatic fragment (dNH⋯O ∼ 2 Å). Adjacent dimer molecules are prone to form supramolecular assemblies due to both hydrophobic alkyl side-chain/side-chain interactions and intermolecular H-bonding.

Original languageEnglish (US)
Pages (from-to)3705-3709
Number of pages5
JournalTetrahedron Letters
Volume52
Issue number29
DOIs
StatePublished - Jul 20 2011

Keywords

  • Aromatic oligoamides
  • Helical arrangement
  • Hydrophobic interactions
  • Self-assembly

ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry

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