A novel peptide conformation: the γ-bend ribbon. Issue 42 (15th October 2018)

• Record Type: Journal Article
• Authors: Drouillat, Bruno; Peggion, Cristina; Biondi, Barbara; Wright, Karen; Couty, François; Crisma, Marco; Formaggio, Fernando; Toniolo, Claudio
• Is Part Of: Organic & biomolecular chemistry. Volume 16:Issue 42(2018)
• Page Start: 7947
• Page End: 7958
• Publication Date: 2018-10-15
• Subjects: Chemistry, Organic -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1039/c8ob02279h
• Languages: English
• ISSNs: 1477-0520

Abstract

Abstract : Conformational analysis of oligopeptides based on the repeating –( S )-(αMe)Aze-( S )-Ala– dyad allowed the characterization of a 3D-structure featuring multiple, non-consecutive γ-bends. 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, C α -tetrasubstituted, N -alkylated α-amino acid residue ( S )- C α -methyl-azetidine-carboxylic acid.