In this study, the functional interaction of HPLW peptide with VEGFR2 (Vascular Endothelial Growth Factor Receptor 2) was determined by using fast 15N-edited NMR spectroscopic experiments. To this aim, 15N uniformly labeled HPLW has been added to Porcine Aortic Endothelial Cells. The acquisition of isotope-edited NMR spectroscopic experiments, including 15N 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 / D. Diana, A. Russomanno, L. De Rosa, R. Di Stasi, D. Capasso, S. Di Gaetano, A. Romanelli, L. Russo, L.D. D'Andrea, R. Fattorusso. - 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
A. Romanelli;
2015
Abstract
In this study, the functional interaction of HPLW peptide with VEGFR2 (Vascular Endothelial Growth Factor Receptor 2) was determined by using fast 15N-edited NMR spectroscopic experiments. To this aim, 15N uniformly labeled HPLW has been added to Porcine Aortic Endothelial Cells. The acquisition of isotope-edited NMR spectroscopic experiments, including 15N relaxation measurements, allowed a precise characterization of the in-cell HPLW epitope recognized by VEGFR2.
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