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Issue 50, 2016
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13-Helix folding of a β/γ-peptide manifold designed from a “minimal-constraint” blueprint

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Abstract

A bottom-up design rationale was adopted to devise β/γ-peptide foldamer manifolds which would adopt preferred 13-helix conformations, relying on minimal steric imposition brought by the constituent amino acid residues. In this way, a well-defined 13-helix conformer was revealed for short oligomers of trans-2-aminocyclobutanecarboxylic acid and γ4-amino acids in alternation, which gave good topological superposition upon an α-helix motif.

Graphical abstract: 13-Helix folding of a β/γ-peptide manifold designed from a “minimal-constraint” blueprint

  • This article is part of the themed collection: Foldamers
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Publication details

The article was received on 10 Mar 2016, accepted on 09 May 2016 and first published on 12 May 2016


Article type: Communication
DOI: 10.1039/C6CC02142E
Citation: Chem. Commun., 2016,52, 7802-7805
  • Open access: Creative Commons BY license
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    13-Helix folding of a β/γ-peptide manifold designed from a “minimal-constraint” blueprint

    C. M. Grison, S. Robin and D. J. Aitken, Chem. Commun., 2016, 52, 7802
    DOI: 10.1039/C6CC02142E

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