Rational design of conformationally constrained cyclopentapeptide antagonists for C-x-C chemokine receptor 4 (CXCR4)

J Med Chem. 2012 Nov 26;55(22):10287-91. doi: 10.1021/jm300926y. Epub 2012 Oct 22.

Abstract

In the absence of an experimentally determined binding mode for the cyclopentapeptide CXCR4 antagonists, we have rationally designed conformationally constrained analogues to further probe the small peptide binding pocket of CXCR4. Two different rigidification strategies were employed, both resulting in highly potent ligands (9 and 13). The information provided by this cyclopentapeptide ligand series will be very valuable in the development of novel peptidomimetic CXCR4 antagonists.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Drug Design*
  • Humans
  • Ligands
  • Models, Molecular
  • Molecular Conformation
  • Peptides, Cyclic / chemical synthesis
  • Peptides, Cyclic / pharmacology*
  • Peptidomimetics*
  • Protein Conformation
  • Receptors, CXCR4 / antagonists & inhibitors*
  • Receptors, CXCR4 / metabolism

Substances

  • Ligands
  • Peptides, Cyclic
  • Peptidomimetics
  • Receptors, CXCR4
  • cyclo(4-amino-1-carbamimidoylpiperidine-4-carboxylic acid-arginyl-3-(2-naphthyl)alanyl-glycyl-tyrosyl)