title: Weak backbone CH···O=C and side chain tBu···tBu London interactions help promote helix folding of achiral NtBu peptoids.
abstract: The synthesis of all-cis amide (NtBu)-glycine oligomers up to 15 residues long by a blockwise coupling approach is reported. The structure and dynamical behavior of these peptoids have been studied by X-ray crystallography, NMR and molecular modeling. Analyses reveal that the folding of these oligomers is driven by weak CH···O=C hydrogen bonding along the peptoid backbone and London interaction between tBu···tBu side-chains.
authors.affiliation: Université Clermont Auvergne, Université Blaise Pascal, Institut de Chimie de Clermont-Ferrand, BP 10448, F-63000 Clermont-Ferrand, France and CNRS, UMR 6296, ICCF, F-63178 Aubière Cedex, France. claude.taillefumier@univ-bpclermont.fr.
authors.forename: G
authors.initials: G
authors.lastname: Angelici
authors.affiliation: Université de Toulouse-INSA-UPS, LPCNO, CNRS UMR 5215, 135 av. Rangueil, F-31077, Toulouse, France and ICBMS UMR 5246, Université de Lyon, Bât. Curien, 43 Bd. du 11 Novembre 1918, 69622 Villeurbanne cedex, France. lionel.perrin@univ-lyon1.fr.
authors.forename: N
authors.initials: N
authors.lastname: Bhattacharjee
authors.affiliation: Université Clermont Auvergne, Université Blaise Pascal, Institut de Chimie de Clermont-Ferrand, BP 10448, F-63000 Clermont-Ferrand, France and CNRS, UMR 6296, ICCF, F-63178 Aubière Cedex, France. claude.taillefumier@univ-bpclermont.fr.
authors.forename: O
authors.initials: O
authors.lastname: Roy
authors.affiliation: Université Clermont Auvergne, Université Blaise Pascal, Institut de Chimie de Clermont-Ferrand, BP 10448, F-63000 Clermont-Ferrand, France and CNRS, UMR 6296, ICCF, F-63178 Aubière Cedex, France. claude.taillefumier@univ-bpclermont.fr.
authors.forename: S
authors.initials: S
authors.lastname: Faure
authors.affiliation: LCM3B, Université de Lorraine, UMR CNRS 7036 CRM2, F-54506 Vandoeuvre-lès-Nancy, France.
authors.forename: C
authors.initials: C
authors.lastname: Didierjean
authors.affiliation: Université Clermont Auvergne, Université Blaise Pascal, Institut de Chimie de Clermont-Ferrand, BP 10448, F-63000 Clermont-Ferrand, France and CNRS, UMR 6296, ICCF, F-63178 Aubière Cedex, France. claude.taillefumier@univ-bpclermont.fr.
authors.forename: L
authors.initials: L
authors.lastname: Jouffret
authors.affiliation: Université de Toulouse-INSA-UPS, LPCNO, CNRS UMR 5215, 135 av. Rangueil, F-31077, Toulouse, France.
authors.forename: F
authors.initials: F
authors.lastname: Jolibois
authors.affiliation: ICBMS UMR 5246, Université de Lyon, Bât. Curien, 43 Bd. du 11 Novembre 1918, 69622 Villeurbanne cedex, France. lionel.perrin@univ-lyon1.fr.
authors.forename: L
authors.initials: L
authors.lastname: Perrin
authors.affiliation: Université Clermont Auvergne, Université Blaise Pascal, Institut de Chimie de Clermont-Ferrand, BP 10448, F-63000 Clermont-Ferrand, France and CNRS, UMR 6296, ICCF, F-63178 Aubière Cedex, France. claude.taillefumier@univ-bpclermont.fr.
authors.forename: C
authors.initials: C
authors.lastname: Taillefumier
mesh_terms: D018360:Crystallography, X-Ray; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D066244:Proton Magnetic Resonance Spectroscopy; D013237:Stereoisomerism
chemical_list: D010455:Peptides