The design, structural and biological characterization of a novel VEGF inhibitor peptide is described. The peptide was designed on the β5-β6 hairpin region of Placenta Growth Factor. NMR studies showed that the peptide assumes in solution a β-hairpin conformation similarly to the corresponding region of the natural ligand. In vitro experiments on endothelial cells demonstrated that the peptide is able to inhibit VEGF biological activity. This molecule represents a novel molecular entity to modulate VEGF activity and with potential application in therapy and diagnosis of angiogenesis-dependent diseases.
Design, structural and biological characterization of a VEGF inhibitor β-hairpin-constrained peptide
BASILE, ANNA;TURCO, Maria Caterina;
2014-01-01
Abstract
The design, structural and biological characterization of a novel VEGF inhibitor peptide is described. The peptide was designed on the β5-β6 hairpin region of Placenta Growth Factor. NMR studies showed that the peptide assumes in solution a β-hairpin conformation similarly to the corresponding region of the natural ligand. In vitro experiments on endothelial cells demonstrated that the peptide is able to inhibit VEGF biological activity. This molecule represents a novel molecular entity to modulate VEGF activity and with potential application in therapy and diagnosis of angiogenesis-dependent diseases.File in questo prodotto:
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