Double-sided α-helix mimetics

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 o...

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Bibliographic Details
Published in:	Tetrahedron Vol. 68; no. 23; pp. 4501 - 4505
Main Authors:	Thompson, Sam, Vallinayagam, Ramakrishnan, Adler, Marc J., Scott, Richard T.W., Hamilton, Andrew D.
Format:	Journal Article
Language:	English
Published:	Elsevier Ltd 10-06-2012
Subjects:	Foldamer Helical structure Peptidomimetic Protein–protein interaction Proteomimetic Foldamer Helical structure Peptidomimetic Proteomimetic Protein–protein interaction
Online Access:	Get full text
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Summary:	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. [Display omitted]
ISSN:	0040-4020 1464-5416
DOI:	10.1016/j.tet.2011.11.010