Jump to main content
Jump to site search


A novel peptide conformation: the γ-bend ribbon

Author affiliations

Abstract

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

Back to tab navigation

Supplementary files

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, Advance Article
  •   Request permissions

    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, Advance Article , DOI: 10.1039/C8OB02279H

Search articles by author

Spotlight

Advertisements