title: FT-IR and NMR structural markers for thiazole-based γ-peptide foldamers.
abstract: Nuclear magnetic resonance (NMR) spectroscopy has been established as a potent method for the determination of foldamer structures in solution. However, the NMR techniques could be limited by averaging, so additional experimental techniques are often needed to fully endorse the folding properties of a sequence. We have recently demonstrated that oligo-γ-peptides composed of 4-amino(methyl)-1,3-thiazole-5-carboxylic acids (ATCs) adopt an original helical fold stabilized by hydrogen bonds forming C9pseudocycles. The main objective of the present work is to reinvestigate the folding of ATC oligomer 1 in order to identify reliable FT-IR and NMR structural markers that are of value for tracking the degree of organization of ATC-based peptides.
authors.affiliation: Institut des Biomolécules Max Mousseron, UMR 5247, Université de Montpellier, CNRS, ENSCM, UFR des Sciences Pharmaceutiques et Biologiques, 15 Avenue Charles Flahault, 34093 Montpellier Cedex 5, France. ludovic.maillard@univ-montp1.fr.
authors.forename: C
authors.initials: C
authors.lastname: Bonnel
authors.affiliation: Institut des Biomolécules Max Mousseron, UMR 5247, Université de Montpellier, CNRS, ENSCM, UFR des Sciences Pharmaceutiques et Biologiques, 15 Avenue Charles Flahault, 34093 Montpellier Cedex 5, France. ludovic.maillard@univ-montp1.fr.
authors.forename: B
authors.initials: B
authors.lastname: Legrand
authors.affiliation: LC2 - UMR 5221 Université de Montpellier, CNRS, Place Eugène Bataillon, 34095 Montpellier, France.
authors.forename: J-L
authors.initials: JL
authors.lastname: Bantignies
authors.affiliation: Institut Charles Gerhardt, UMR 5253 CNRS/ENSCM/UM, Matériaux Avancés pour la Catalyse et la Santé, Ecole Nationale Supérieure de Chimie, 8 rue de l'Ecole Normale, 34296 Montpellier Cedex 5, France.
authors.forename: H
authors.initials: H
authors.lastname: Petitjean
authors.affiliation: Institut des Biomolécules Max Mousseron, UMR 5247, Université de Montpellier, CNRS, ENSCM, UFR des Sciences Pharmaceutiques et Biologiques, 15 Avenue Charles Flahault, 34093 Montpellier Cedex 5, France. ludovic.maillard@univ-montp1.fr.
authors.forename: J
authors.initials: J
authors.lastname: Martinez
authors.affiliation: Institut des Biomolécules Max Mousseron, UMR 5247, Université de Montpellier, CNRS, ENSCM, UFR des Sciences Pharmaceutiques et Biologiques, 15 Avenue Charles Flahault, 34093 Montpellier Cedex 5, France. ludovic.maillard@univ-montp1.fr.
authors.forename: N
authors.initials: N
authors.lastname: Masurier
authors.affiliation: Institut des Biomolécules Max Mousseron, UMR 5247, Université de Montpellier, CNRS, ENSCM, UFR des Sciences Pharmaceutiques et Biologiques, 15 Avenue Charles Flahault, 34093 Montpellier Cedex 5, France. ludovic.maillard@univ-montp1.fr.
authors.forename: L T
authors.initials: LT
authors.lastname: Maillard
mesh_terms: D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D057786:Peptidomimetics / Q000737:chemistry*; D000072756:Protein Conformation, alpha-Helical; D017510:Protein Folding; D017550:Spectroscopy, Fourier Transform Infrared; D013844:Thiazoles / Q000737:chemistry*
chemical_list: D010455:Peptides; D057786:Peptidomimetics; D013844:Thiazoles