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Heterochiral Ala/(αMe)Aze sequential oligopeptides: Synthesis and conformational study.

Bruno DrouillatCristina PeggionBarbara BiondiKaren WrightFrançois CoutyMarco CrismaFernando FormaggioClaudio Toniolo
Published in: Journal of peptide science : an official publication of the European Peptide Society (2019)
α-Amino acid residues with a ϕ,ψ constrained conformation are known to significantly bias the peptide backbone 3D structure. An intriguing member of this class of compounds is (αMe)Aze, characterized by an Nα -alkylated four-membered ring and Cα -methylation. We have already reported that (S)-(αMe)Aze, when followed by (S)-Ala in the homochiral dipeptide sequential motif -(S)-(αMe)Aze-(S)-Ala-, tends to generate the unprecedented γ-bend ribbon conformation, as formation of a regular, fully intramolecularly H-bonded γ-helix is precluded, due to the occurrence of a tertiary amide bond every two residues. In this work, we have expanded this study to the preparation and 3D structural analysis of the heterochiral (S)-Ala/(R)-(αMe)Aze sequential peptides from dimer to hexamer. Our conformational results show that members of this series may fold in type-II β-turns or in γ-turns depending on the experimental conditions.
Keyphrases
  • molecular dynamics simulations
  • amino acid
  • molecular dynamics
  • risk assessment
  • single molecule
  • gene expression
  • mass spectrometry
  • liquid chromatography