β-Hairpin stabilization through an interstrand triazole bridge

Chem Commun (Camb). 2012 Jan 18;48(5):762-4. doi: 10.1039/c1cc16017f. Epub 2011 Dec 1.

Abstract

β-Hairpin peptides were conformationally stabilized through a 1,4 disubstituted 1,2,3-triazole interstrand linkage. A NMR conformational analysis revealed that the β-hairpin content depends on the number and position of substituent methylene units of the 1,2,3-triazole ring. These results will allow the design of metabolically stable peptidomimetic analogs of bioactive β-hairpin peptides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chemistry, Pharmaceutical / methods*
  • Magnetic Resonance Spectroscopy
  • Methane / analogs & derivatives
  • Methane / chemistry
  • Peptides / analysis
  • Peptides / chemistry*
  • Peptidomimetics / analysis
  • Peptidomimetics / chemical synthesis*
  • Protein Folding
  • Protein Structure, Secondary
  • Proteins / analysis
  • Proteins / chemistry*
  • Triazoles / chemistry*

Substances

  • Peptides
  • Peptidomimetics
  • Proteins
  • Triazoles
  • Trpzip2 protein
  • methylene radical
  • Methane