%0 Journal Article %T 12/14/14-Helix Formation in 2:1 alpha/beta-Hybrid Peptides Containing Bicyclo[2.2.2]octane Ring Constraints %+ Institut des Biomolécules Max Mousseron [Pôle Chimie Balard] (IBMM) %+ Cristallographie, Résonance Magnétique et Modélisations (CRM2) %+ Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier (ICGM) %+ Laboratoire Charles Coulomb (L2C) %A Legrand, Baptiste %A Andre, Christophe %A Moulat, Laure %A Didierjean, Claude %A Hermet, Patrick %A Bantignies, Jean-Louis %A Martinez, Jean %A Amblard, Muriel %A Calmes, Monique %< avec comité de lecture %@ 0947-6539 %J Chemistry - A European Journal %I Wiley-VCH Verlag %V 22 %P 11986-11990 %8 2016-08-11 %D 2016 %R 10.1002/chem.201602746 %Z Chemical Sciences/Theoretical and/or physical chemistryJournal articles %X The highly constrained b-amino acid ABOC induces different types of helices in b urea and 1:1 a/b amide oligomers. The latter can adopt 11/9- and 18/16-helical folds depending on the chain length in solution. Short peptides alternating proteinogenic a-amino acids and ABOC in a 2:1 a/b repeat pattern adopted an unprecedented and stable 12/14/14-helix. The structure was established through extensive NMR, molecular dynamics, and IR studies. While the 1:1 a-AA/ABOC helices diverged from the canonical a-helix, the helix formed by the 9-mer 2:1 a/b-peptide allowed the projection of the a-aminoacid side chains in a spatial arrangement according to the a-helix. Such a finding constitutes an important step toward the conception of functional tools that use the ABOC residue as a potent helix inducer for biological applications. %G English %L hal-01368422 %U https://hal.science/hal-01368422 %~ CNRS %~ ENSC-MONTPELLIER %~ ICG %~ IBMM %~ L2C %~ UNIV-LORRAINE %~ INC-CNRS %~ CRM2-UL %~ MIPS %~ CHIMIE %~ UNIV-MONTPELLIER %~ UM-2015-2021 %~ TEST2-HALCNRS