• VEGF;
  • angiogenesis;
  • NMR;
  • peptide;
  • interactions

Angiogenesis is mainly regulated by the vascular endothelial growth factor (VEGF), a mitogen specific for endothelial cells, which binds two tyrosine kinase receptors, VEGFR1 and VEGFR2, on the surface of endothelial cells. Molecules targeting VEGF receptors are attractive to pharmacologically treat diseases associated with angiogenesis or to be used as probes in angiogenesis imaging. Recently, we reported a designed peptide targeting VEGF receptors and able to inhibit the VEGF-angiogenic response in vitro and in vivo. In this study, we employed NMR and molecular modeling methodology to investigate the molecular determinants of the interaction peptide-receptor. In particular, the peptide binding site on VEGFR1 domain 2 and the residues involved in receptor recognition have been determined. These results provide significant information to develop a new class of molecules able to recognize the VEGF receptors overexpressed in pathological angiogenesis. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.