Chiral Sulfoxide-Induced Single Turn Peptide α-Helicity

Sci Rep. 2016 Dec 9:6:38573. doi: 10.1038/srep38573.

Abstract

Inducing α-helicity through side-chain cross-linking is a strategy that has been pursued to improve peptide conformational rigidity and bio-availability. Here we describe the preparation of small peptides tethered to chiral sulfoxide-containing macrocyclic rings. Furthermore, a study of structure-activity relationships (SARs) disclosed properties with respect to ring size, sulfur position, oxidation state, and stereochemistry that show a propensity to induce α-helicity. Supporting data include circular dichroism spectroscopy (CD), NMR spectroscopy, and a single crystal X-ray structure for one such stabilized peptide. Finally, theoretical studies are presented to elucidate the effect of chiral sulfoxides in inducing backbone α-helicity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Circular Dichroism
  • Models, Molecular
  • Oxidation-Reduction
  • Peptides / chemistry*
  • Protein Conformation, alpha-Helical*
  • Safrole / analogs & derivatives*
  • Safrole / chemistry

Substances

  • Peptides
  • Safrole
  • sulfoxide