%0 Journal Article
%T FT-​IR and NMR structural markers for thiazole-​based γ-​peptide foldamers
%+ Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM)
%+ Laboratoire Charles Coulomb (L2C)
%+ Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier (ICGM)
%A Bonnel, Clément
%A Legrand, Baptiste
%A Bantignies, Jean-Louis
%A Petitjean, Hugo
%A Martinez, Jean
%A Masurier, Nicolas
%A Maillard, Ludovic T
%< avec comité de lecture
%@ 1477-0520
%J Organic & Biomolecular Chemistry
%I Royal Society of Chemistry
%V 14
%N 37
%P 8664
%8 2016
%D 2016
%R 10.1039/C6OB01594H
%Z Chemical Sciences/Theoretical and/or physical chemistry
%Z Chemical Sciences/Organic chemistryJournal articles
%X NMR spectroscopy has been established as a potent method for the detn. of foldamer structures in soln. However, the NMR techniques could be limited by averaging, so addnl. exptl. techniques are often needed to fully endorse the folding properties of a sequence. The authors 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 C9 pseudocycles. The main objective of the present work is to restudy the folding of ATC oligomer 1 to identify reliable FTIR and NMR structural markers that are of value for tracking the degree of organization of ATC-​based peptides.
%G English
%L hal-01398165
%U https://hal.science/hal-01398165
%~ CNRS
%~ ENSC-MONTPELLIER
%~ ICG
%~ IBMM
%~ L2C
%~ INC-CNRS
%~ MIPS
%~ CHIMIE
%~ UNIV-MONTPELLIER
%~ ANR
%~ UM-2015-2021