Flow-chemistry enabled efficient synthesis of β-peptides: backbone topology vs. helix formation

Chem Commun (Camb). 2019 Mar 7;55(21):3061-3064. doi: 10.1039/c8cc10147g.

Abstract

Enantiodiscriminative helix formation was observed for β-peptide H14 helices. This observation is caused by the synperiplanar orientation of H-O atoms which is more unfavorable than those for H-H interaction. The 1,2 H-O interaction leads to the destruction of the helical structure. The introduction of a double C-C bond in the backbone rules out helix formation.

MeSH terms

  • Hydrogen Bonding
  • Models, Molecular
  • Oligopeptides / chemical synthesis*
  • Oligopeptides / chemistry
  • Protein Conformation, alpha-Helical
  • Protein Conformation, beta-Strand
  • Protein Folding

Substances

  • Oligopeptides