1,2,3-Triazole Bridge as Conformational Constrain in β-Hairpin Peptides: Analysis of Hydrogen-Bonded Positions

Chemistry. 2016 Apr 11;22(16):5534-7. doi: 10.1002/chem.201600154. Epub 2016 Mar 3.

Abstract

Conformational constrained β-hairpin peptides are useful tool to modulate protein-protein interactions. A triazole bridge in hydrogen-bonded positions between two antiparallel strands induces a conformational stabilization of the β-hairpin peptide. The entity of the stability of the β-hairpin peptide depends on the length of the bridge.

Keywords: NMR spectroscopy; click chemistry; cycloaddition; peptidomimetics; β-hairpin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Peptides / chemistry*
  • Protein Conformation
  • Triazoles / chemistry*

Substances

  • Peptides
  • Triazoles