title: α-Peptide-Oligourea Chimeras: Stabilization of Short α-Helices by Non-Peptide Helical Foldamers.
abstract: Short α-peptides with less than 10 residues generally display a low propensity to nucleate stable helical conformations. While various strategies to stabilize peptide helices have been previously reported, the ability of non-peptide helical foldamers to stabilize α-helices when fused to short α-peptide segments has not been investigated. Towards this end, structural investigations into a series of chimeric oligomers obtained by joining aliphatic oligoureas to the C- or N-termini of α-peptides are described. All chimeras were found to be fully helical, with as few as 2 (or 3) urea units sufficient to propagate an α-helical conformation in the fused peptide segment. The remarkable compatibility of α-peptides with oligoureas described here, along with the simplicity of the approach, highlights the potential of interfacing natural and non-peptide backbones as a means to further control the behavior of α-peptides.
authors.affiliation: Univ. Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie (IECB), 2 rue Robert Escarpit, 33607 Pessac (France).|CNRS, CBMN, UMR 5248, 33600 Pessac (France).|UREkA, Sarl, 2 rue Robert Escarpit, 33607 Pessac (France).
authors.forename: Juliette
authors.initials: J
authors.lastname: Fremaux
authors.affiliation: Univ. Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie (IECB), 2 rue Robert Escarpit, 33607 Pessac (France).|CNRS, CBMN, UMR 5248, 33600 Pessac (France).|UREkA, Sarl, 2 rue Robert Escarpit, 33607 Pessac (France).
authors.forename: Laura
authors.initials: L
authors.lastname: Mauran
authors.affiliation: Univ. Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie (IECB), 2 rue Robert Escarpit, 33607 Pessac (France).|CNRS, CBMN, UMR 5248, 33600 Pessac (France).|Present address: Faculty of Chemistry, University of Warsaw, Pasteura 1, 02-093 Warsaw (Poland).
authors.forename: Karolina
authors.initials: K
authors.lastname: Pulka-Ziach
authors.affiliation: Univ. Bordeaux, IECB, UMS 3033/US 001, 2 rue Escarpit, 33607 Pessac (France).|CNRS, IECB, UMS 3033, 33600 Pessac (France).|INSERM, IECB, US 001, 33600 Pessac (France).
authors.forename: Brice
authors.initials: B
authors.lastname: Kauffmann
authors.affiliation: CNRS, CBMN, UMR 5248, 33600 Pessac (France).|Univ. Bordeaux, CBMN, UMR 5248, All. Geoffroy Saint-Hilaire, 33600 Pessac (France).
authors.forename: Benoit
authors.initials: B
authors.lastname: Odaert
authors.affiliation: Univ. Bordeaux, CBMN, UMR 5248, Institut Européen de Chimie et Biologie (IECB), 2 rue Robert Escarpit, 33607 Pessac (France). g.guichard@iecb.u-bordeaux.fr.|CNRS, CBMN, UMR 5248, 33600 Pessac (France). g.guichard@iecb.u-bordeaux.fr.
authors.forename: Gilles
authors.initials: G
authors.lastname: Guichard
mesh_terms: D018360:Crystallography, X-Ray; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D055550:Protein Stability; D017433:Protein Structure, Secondary; D014508:Urea / Q000737:chemistry*
chemical_list: D010455:Peptides; D014508:Urea
keywords: X-ray crystallography; foldamers; helices; oligourea; peptides