Double-sided α-helix mimetics

Sam Thompson, Ramakrishnan Vallinayagam, Marc J. Adler, Richard T.W. Scott, Andrew D. Hamilton

Research output: Contribution to journalArticle

Abstract

The design and synthesis of substituted bis- and tris-benzamides is reported in which the projection of side-chain residues on both sides of an α-helix is reproduced. The scaffold is conformationally constrained by a series of intramolecular hydrogen bonds, allowing for spatial and angular mimicry of the i, i+2, i+4 and i+6 side-chains in the case of the bis-benzamide, and may be extended to higher-order oligomers.

Original languageEnglish (US)
Pages (from-to)4501-4505
Number of pages5
JournalTetrahedron
Volume68
Issue number23
DOIs
StatePublished - Jun 10 2012

Keywords

  • Foldamer
  • Helical structure
  • Peptidomimetic
  • Protein-protein interaction
  • Proteomimetic

ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry

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    Thompson, S., Vallinayagam, R., Adler, M. J., Scott, R. T. W., & Hamilton, A. D. (2012). Double-sided α-helix mimetics. Tetrahedron, 68(23), 4501-4505. https://doi.org/10.1016/j.tet.2011.11.010