http://www.cnr.it/ontology/cnr/individuo/prodotto/ID184563
Characterization of a Designed Vascular Endothelial Growth Factor Receptor Antagonist Helical Peptide with Antiangiogenic Activity in Vivo (Articolo in rivista)
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- Characterization of a Designed Vascular Endothelial Growth Factor Receptor Antagonist Helical Peptide with Antiangiogenic Activity in Vivo (Articolo in rivista) (literal)
- Anno
- 2011-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/jm101435r (literal)
- Alternative label
Basile, A; Del Gatto, A; Diana, D; Di Stasi, R; Falco, A; Festa, M; Rosati, A; Barbieri, A; Franco, R; Arra, C; Pedone, C; Fattorusso, R; Turco, MC; D'Andrea, LD (2011)
Characterization of a Designed Vascular Endothelial Growth Factor Receptor Antagonist Helical Peptide with Antiangiogenic Activity in Vivo
in Journal of medicinal chemistry; American Chemical Society, Washington (Stati Uniti d'America)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Basile, A; Del Gatto, A; Diana, D; Di Stasi, R; Falco, A; Festa, M; Rosati, A; Barbieri, A; Franco, R; Arra, C; Pedone, C; Fattorusso, R; Turco, MC; D'Andrea, LD (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1. CNR, Ist Biostrutture & Bioimmagini, I-80134 Naples, Italy
2. Univ Salerno, Dipartimento Sci Farmaceut, Salerno, Italy
3. Fdn G Pascale, Ist Nazl Tumori, Naples, Italy
4. Univ Naples Federico 2, Dipartimento Sci Biol, Naples, Italy
5. Seconda Univ Napoli, Dipartimento Sci Ambientali, Caserta, Italy (literal)
- Titolo
- Characterization of a Designed Vascular Endothelial Growth Factor Receptor Antagonist Helical Peptide with Antiangiogenic Activity in Vivo (literal)
- 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. (literal)
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