Diphenylacetylene-linked peptide strands induce bidirectional β-sheet formation

Angew Chem Int Ed Engl. 2014 Apr 1;53(14):3650-3. doi: 10.1002/anie.201309353. Epub 2014 Feb 19.

Abstract

In the search for synthetic mimics of protein secondary structures relevant to the mediation of protein-protein interactions, we have synthesized a series of tetrasubstituted diphenylacetylenes that display β-sheet structures in two directions. Extensive X-ray crystallographic and NMR solution phase studies are consistent with these proteomimetics adopting sheet structures, displaying both hydrophobic and hydrophilic amino acid side chains.

Keywords: beta-sheets; peptidomimetics; protein surfaces; protein-protein interactions; secondary structures.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylene / analogs & derivatives*
  • Acetylene / chemistry
  • Crystallography, X-Ray
  • Hydrogen Bonding
  • Hydrophobic and Hydrophilic Interactions
  • Peptides / chemistry
  • Protein Folding
  • Protein Unfolding

Substances

  • Peptides
  • biphenylacetylene
  • Acetylene