Special issue devoted to contributions presented at the 13th Naples Workshop on Bioactive Peptides, June 7–10, 2012.
Special Issue Article
Structural investigation of the VEGF receptor interaction with a helical antagonist peptide†
Version of Record online: 19 FEB 2013
Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.
Journal of Peptide Science
Special Issue: Special issue devoted to contributions presented at the 13th Naples Workshop on Bioactive Peptides, June 7–10, 2012, Naples
Volume 19, Issue 4, pages 214–219, April 2013
How to Cite
Diana, D., Di Stasi, R., De Rosa, L., Isernia, C., D'Andrea, L. D. and Fattorusso, R. (2013), Structural investigation of the VEGF receptor interaction with a helical antagonist peptide. J. Peptide Sci., 19: 214–219. doi: 10.1002/psc.2480
- Issue online: 24 MAR 2013
- Version of Record online: 19 FEB 2013
- Manuscript Accepted: 17 DEC 2012
- Manuscript Revised: 15 DEC 2012
- Manuscript Received: 18 OCT 2012
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.