Characterization of a designed vascular endothelial growth factor receptor antagonist helical peptide with antiangiogenic activity in Vivo

Anna Basile, Annarita Del Gatto, Donatella Diana, Rossella Di Stasi, Antonia Falco, Michelina Festa, Alessandra Rosati, Antonio Barbieri, Renato Franco, Claudio Arra, Carlo Pedone, Roberto Fattorusso, Maria Caterina Turco, Luca Domenico D'Andrea

Research output: Contribution to journalArticlepeer-review

Abstract

Angiogenesis is a fundamental process underlining physiological and pathological conditions. It is mainly regulated by the vascular endothelial growth factor (VEGF) and its receptors, which are the main targets of molecules able to modulate the angiogenic response. Pharmaceutical therapies based on antiangiogenic drugs represent a promising approach for the treatment of several socially important diseases. We report the biological and structural characterization of a VEGF receptor binder peptide designed on the N-terminal helix of VEGF. The reported experimental evidence shows that the peptide assumes in water a well-defined helical conformation and indicates that this peptide is a VEGF receptor antagonist and possesses antiangiogenic biological activity. In particular, it inhibits VEGF stimulated endothelial cell proliferation, activation, and survival, as well as angiogenesis and tumor progression in vivo. This peptide is a candidate for the development of novel peptide-based drugs for the treatment of diseases associated with excessive VEGF-dependent angiogenesis.

Original languageEnglish
Pages (from-to)1391-1400
Number of pages10
JournalJournal of Medicinal Chemistry
Volume54
Issue number5
DOIs
Publication statusPublished - Mar 10 2011

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery

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