http://www.cnr.it/ontology/cnr/individuo/prodotto/ID184559

beta-Hairpin Peptide That Targets Vascular Endothelial Growth Factor (VEGF) Receptors: DESIGN, NMR CHARACTERIZATION, AND BIOLOGICAL ACTIVITY (Articolo in rivista)

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beta-Hairpin Peptide That Targets Vascular Endothelial Growth Factor (VEGF) Receptors: DESIGN, NMR CHARACTERIZATION, AND BIOLOGICAL ACTIVITY (Articolo in rivista) (literal)

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Alternative label

Diana, D; Basile, A; De Rosa, L; Di Stasi, R; Auriemma, S; Arra, C; Pedone, C; Turco, MC; Fattorusso, R; D'Andrea, LD (2011)
beta-Hairpin Peptide That Targets Vascular Endothelial Growth Factor (VEGF) Receptors: DESIGN, NMR CHARACTERIZATION, AND BIOLOGICAL ACTIVITY
in The Journal of biological chemistry (Print); American Society Of Biochemistry And Molecular Biology Inc. (ASBMB), Rockville (Stati Uniti d'America)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Diana, D; Basile, A; De Rosa, L; Di Stasi, R; Auriemma, S; Arra, C; Pedone, C; Turco, MC; Fattorusso, R; D'Andrea, LD (literal)

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Note

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1. CNR, Ist Biostrutture & Bioimmagini, I-80134 Naples, Italy 2. Univ Salerno, Dipartimento Sci Farmaceut & Biomed, I-84084 Salerno, Italy 3. Univ Naples Federico 2, Dipartimento Sci Biol, I-80134 Naples, Italy 4. Ist Nazl Tumori Fdn G Pascale, I-80131 Naples, Italy 5. Univ Naples 2, Dipartimento Sci Ambientali, I-81100 Caserta, Italy (literal)

Titolo

beta-Hairpin Peptide That Targets Vascular Endothelial Growth Factor (VEGF) Receptors: DESIGN, NMR CHARACTERIZATION, AND BIOLOGICAL ACTIVITY (literal)

Abstract

VEGF receptors have been the target of intense research aimed to develop molecules able to inhibit or stimulate angiogenesis. Based on the x-ray structure of the complex placental growth factor-VEGF receptor 1,2, we designed a VEGF receptor-binding peptide reproducing the placental growth factor beta-hairpin region Gln(87)-Val(100) that is involved in receptor recognition. A conformational analysis showed that the designed peptide adopts the expected fold in pure water. Moreover, a combination of NMR interaction analysis and cell binding studies were used to demonstrate that the peptide targets VEGF receptors. The VEGF receptor 1(D2)-interacting residues were characterized at the molecular level, and they correspond to the residues recognizing the placental growth factor sequence Gln(87)-Val(100). Finally, the peptide biological activity was characterized in vitro and in vivo, and it showed a VEGF-like behavior. Indeed, the peptide activated VEGF-dependent intracellular pathways, induced endothelial cell proliferation and rescue from apoptosis, and promoted angiogenesis in vivo. This compound is one of the few peptides known with proangiogenic activity, which makes it a candidate for the development of a novel peptide-based drug for medical applications in therapeutic angiogenesis. (literal)

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