Structure-based design of a bicyclic peptide antagonist of the vascular endothelial growth factor receptors

J Pept Sci. 2008 Jun;14(6):767-72. doi: 10.1002/psc.965.

Abstract

Dysregulated angiogenesis is implicated in several pathologies, including cancer and age-related macular degeneration. A potential antiangiogenic strategy consists in developing VEGF receptor ligands capable of preventing VEGF binding and the subsequent activation of these receptors. Herein, we describe the structure-based design of a VEGF-mimicking peptide, VG3F. This 25-mer peptide was doubly cyclized, on-resin, by formation of both a disulfide bridge and an intramolecular amide bond to constrain it to adopt a bioactive conformation. Tested on in vitro assays, VG3F was able to prevent VEGF binding to VEGF receptor 1 and inhibit both VEGF-induced signal transduction and cell migration.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Line
  • Drug Design*
  • Humans
  • Luminescence
  • Models, Molecular
  • Molecular Sequence Data
  • Peptides, Cyclic / chemical synthesis*
  • Peptides, Cyclic / pharmacology
  • Protein Conformation
  • Receptors, Vascular Endothelial Growth Factor / antagonists & inhibitors*

Substances

  • Peptides, Cyclic
  • Receptors, Vascular Endothelial Growth Factor