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Issue 90, 2015
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The discovery of 9/8-ribbons, β/γ-peptides with curved shapes governed by a combined configuration-conformation code

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Abstract

The de novo design of a β/γ-peptidic foldamer motif has led to the discovery of an unprecedented 9/8-ribbon featuring an uninterrupted alternating C9/C8 hydrogen-bonding network. The ribbons adopt partially curved topologies determined synchronistically by the β-residue configuration and the γ-residue conformation sets.

Graphical abstract: The discovery of 9/8-ribbons, β/γ-peptides with curved shapes governed by a combined configuration-conformation code

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

The article was received on 25 Aug 2015, accepted on 15 Sep 2015 and first published on 15 Sep 2015


Article type: Communication
DOI: 10.1039/C5CC07136D
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Citation: Chem. Commun., 2015,51, 16233-16236
  • Open access: Creative Commons BY-NC license
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    The discovery of 9/8-ribbons, β/γ-peptides with curved shapes governed by a combined configuration-conformation code

    C. M. Grison, S. Robin and D. J. Aitken, Chem. Commun., 2015, 51, 16233
    DOI: 10.1039/C5CC07136D

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