4.4 Article

Double-sided α-helix mimetics

Journal

TETRAHEDRON
Volume 68, Issue 23, Pages 4501-4505

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.tet.2011.11.010

Keywords

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

Funding

  1. University of Oxford

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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 alpha-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. (C) 2011 Elsevier Ltd. All rights reserved.

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