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Issue 42, 2018
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A novel peptide conformation: the γ-bend ribbon

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Unlike the extensively investigated relationship between the peptide β-bend ribbon and its prototypical 310-helix conformation, the corresponding relationship between the narrower γ-bend ribbon and its regular γ-helix counterpart still remains to be studied, as the latter 3D-structures have not yet been experimentally authenticated. In this paper, we describe the results of the first characterization, both in the crystal state and in solution, of the γ-bend ribbon conformation using X-ray diffraction and FT-IR absorption, electronic CD and 2D-NMR spectroscopies applied to an appropriate set of synthetic, homo-chiral, sequential dipeptide oligomers based on (S)-Ala and the known γ-bend inducer, Cα-tetrasubstituted, N-alkylated α-amino acid residue (S)-Cα-methyl-azetidine-carboxylic acid.

Graphical abstract: A novel peptide conformation: the γ-bend ribbon

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Publication details

The article was received on 14 Sep 2018, accepted on 09 Oct 2018 and first published on 09 Oct 2018

Article type: Paper
DOI: 10.1039/C8OB02279H
Citation: Org. Biomol. Chem., 2018,16, 7947-7958

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    A novel peptide conformation: the γ-bend ribbon

    B. Drouillat, C. Peggion, B. Biondi, K. Wright, F. Couty, M. Crisma, F. Formaggio and C. Toniolo, Org. Biomol. Chem., 2018, 16, 7947
    DOI: 10.1039/C8OB02279H

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