title: Conformation control of abiotic α-helical foldamers.
abstract: With the aim to find new protein-protein inhibitors, a three part methodology was applied to oligophenylpyridines. Theoretical ring twist angle predictions have been validated by X-ray diffraction and molecular dynamics simulations with NMR constraints. Careful choice of substituent and nitrogen positions in oligophenylpyridyl foldamer units opens the way to conformational control of the side chain distribution of this α-helix mimic.
authors.affiliation: Normandie Université , France.
authors.forename: Serge
authors.initials: S
authors.lastname: Perato
authors.forename: Jade
authors.initials: J
authors.lastname: Fogha
authors.forename: Muriel
authors.initials: M
authors.lastname: Sebban
authors.forename: Anne Sophie
authors.initials: AS
authors.lastname: Voisin-Chiret
authors.forename: Jana
authors.initials: J
authors.lastname: Sopkova-de Oliveira Santos
authors.forename: Hassan
authors.initials: H
authors.lastname: Oulyadi
authors.forename: Sylvain
authors.initials: S
authors.lastname: Rault
mesh_terms: D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008968:Molecular Conformation; D056004:Molecular Dynamics Simulation; D018716:Molecular Mimicry; D011506:Proteins / Q000737:chemistry*; D011725:Pyridines / Q000737:chemistry*; D054852:Small Molecule Libraries / Q000737:chemistry*; D013329:Structure-Activity Relationship; D013816:Thermodynamics
chemical_list: D011506:Proteins; D011725:Pyridines; D054852:Small Molecule Libraries