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 beta-hairpin VEGF receptor targeting peptide determined by nmr spectroscopy in living cells
Diana D;De Rosa L;Di Stasi R;Di Gaetano S;D'Andrea LD;
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.File in questo prodotto:
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Descrizione: Functional binding surface of a beta-hairpin VEGF receptor targeting peptide determined by nmr spectroscopy in living cells
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