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, D., Russomanno, A., DE ROSA, L., Di Stasi, R., Capasso, D., DI GAETANO, S., Romanelli, A., Russo, L., D'Andrea, L.D., Fattorusso, R.. - 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.
