%0 Journal Article
%T Prospect of Thiazole‐based γ‐Peptide Foldamers in Enamine Catalysis: Exploration of the Nitro‐Michael Addition
%+ Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM)
%+ Laboratoire Charles Coulomb (L2C)
%+ Chungbuk National University
%+ Elettra Sincrotrone Trieste
%+ Institut Européen des membranes (IEM)
%+ Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier (ICGM)
%A Aguesseau‐kondrotas, Julie
%A Simon, Matthieu
%A Legrand, Baptiste
%A Bantigniès, Jean‐louis
%A Kang, Young Kee
%A Dumitrescu, Dan
%A Van der lee, Arie
%A Campagne, Jean‐marc
%A de Figueiredo, Renata Marcia
%A Maillard, Ludovic
%< avec comité de lecture
%@ 0947-6539
%J Chemistry - A European Journal
%I Wiley-VCH Verlag
%V 25
%N 30
%P 7396-7401
%8 2019-03-18
%D 2019
%R 10.1002/chem.201901221
%K catalysis
%K enamines
%K foldamers
%K helical structures
%K γ-peptides
%Z Chemical Sciences
%Z Chemical Sciences/CatalysisJournal articles
%X As three‐dimensional folding is prerequisite to biopolymer activity, complex functions may also be achieved through foldamer science. Because of the diversity of sizes, shapes and folding available with synthetic monomers, foldamer frameworks enable a numerous opportunities for designing new generations of catalysts. We herein demonstrate that heterocyclic γ‐peptide scaffolds represent a versatile platform for enamine catalysis. One central feature was to determine how the catalytic activity and the transfer of chiral information might be under the control of the conformational behaviours of the oligomer.
%G English
%L hal-02167326
%U https://hal.umontpellier.fr/hal-02167326
%~ CNRS
%~ ENSC-MONTPELLIER
%~ ICG
%~ IBMM
%~ IEM
%~ L2C
%~ INC-CNRS
%~ MIPS
%~ CHIMIE
%~ UNIV-MONTPELLIER
%~ TEST-HALCNRS
%~ ANR
%~ UM-2015-2021
%~ BIOLOGIE_ET_AMELIORATION_DES_PLANTES