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12/14/14‐Helix Formation in 2:1 α/β‐Hybrid Peptides Containing Bicyclo[2.2.2]octane Ring Constraints
Author(s) -
Legrand Baptiste,
André Christophe,
Moulat Laure,
Didierjean Claude,
Hermet Patrick,
Bantignies JeanLouis,
Martinez Jean,
Amblard Muriel,
Calmès Monique
Publication year - 2016
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201602746
Subject(s) - helix (gastropod) , chemistry , stereochemistry , ring (chemistry) , amino acid , peptide , amide , octane , molecular dynamics , side chain , crystallography , biochemistry , biology , computational chemistry , organic chemistry , polymer , ecology , snail
Abstract The highly constrained β‐amino acid ABOC induces different types of helices in β urea and 1:1 α/β amide oligomers. The latter can adopt 11/9‐ and 18/16‐helical folds depending on the chain length in solution. Short peptides alternating proteinogenic α‐amino acids and ABOC in a 2:1 α/β 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 α‐AA/ABOC helices diverged from the canonical α‐helix, the helix formed by the 9‐mer 2:1 α/β‐peptide allowed the projection of the α‐amino acid side chains in a spatial arrangement according to the α‐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.