12/14/14-Helix Formation in 2:1 alpha/beta-Hybrid Peptides Containing Bicyclo[2.2.2]octane Ring Constraints - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue Chemistry - A European Journal Année : 2016

12/14/14-Helix Formation in 2:1 alpha/beta-Hybrid Peptides Containing Bicyclo[2.2.2]octane Ring Constraints

Résumé

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-amino acid 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.

Dates et versions

hal-01368422 , version 1 (19-09-2016)

Identifiants

Citer

Baptiste Legrand, Christophe Andre, Laure Moulat, Claude Didierjean, Patrick Hermet, et al.. 12/14/14-Helix Formation in 2:1 alpha/beta-Hybrid Peptides Containing Bicyclo[2.2.2]octane Ring Constraints. Chemistry - A European Journal, 2016, 22, pp.11986-11990. ⟨10.1002/chem.201602746⟩. ⟨hal-01368422⟩
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