In this study, the functional interaction of HPLW peptide with VEGFR2 (Vascular Endothelial Growth Factor Receptor 2) was determined by using fast (15)N-edited NMR spectroscopic experiments. To this aim, (15)N uniformly labelled HPLW has been added to Porcine Aortic Endothelial Cells. The acquisition of isotope-edited NMR spectroscopic experiments, including (15)N relaxation measurements, allowed a precise characterization of the in-cell HPLW epitope recognized by VEGFR2.
Functional binding surface of a β-hairpin VEGF receptor targeting peptide determined by NMR spectroscopy in living cells / Diana, Donatella; Russomanno, Anna; DE ROSA, Lucia; Di Stasi, Rossella; Capasso, Domenica; DI GAETANO, Sonia; Romanelli, Alessandra; Russo, Luigi; D'Andrea, LUCA DOMENICO; Fattorusso, Roberto. - In: CHEMISTRY-A EUROPEAN JOURNAL. - ISSN 0947-6539. - 21:1(2015), pp. 91-95. [10.1002/chem.201403335]
Functional binding surface of a β-hairpin VEGF receptor targeting peptide determined by NMR spectroscopy in living cells
DIANA, DONATELLA;DE ROSA, LUCIA;CAPASSO, DOMENICA;DI GAETANO, SONIA;ROMANELLI, ALESSANDRA;D'ANDREA, LUCA DOMENICO;
2015
Abstract
In this study, the functional interaction of HPLW peptide with VEGFR2 (Vascular Endothelial Growth Factor Receptor 2) was determined by using fast (15)N-edited NMR spectroscopic experiments. To this aim, (15)N uniformly labelled HPLW has been added to Porcine Aortic Endothelial Cells. The acquisition of isotope-edited NMR spectroscopic experiments, including (15)N relaxation measurements, allowed a precise characterization of the in-cell HPLW epitope recognized by VEGFR2.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
