Functional binding surface of a β-hairpin VEGF receptor targeting peptide determined by NMR spectroscopy in living cells.
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.
Istituto di Biostrutture e Bioimmagini, C.N.R., via Mezzocannone 16, 80134, Napoli (Italy).
Donatella
D
Diana
Anna
A
Russomanno
Lucia
L
De Rosa
Rossella
R
Di Stasi
Domenica
D
Capasso
Sonia
S
Di Gaetano
Alessandra
A
Romanelli
Luigi
L
Russo
Luca D
LD
D'Andrea
Roberto
R
Fattorusso
D000818:Animals; D002460:Cell Line; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary; D013552:Swine; D040301:Vascular Endothelial Growth Factor Receptor-2 / Q000819:agonists* / Q000235:genetics / Q000378:metabolism
D009587:Nitrogen Isotopes; D010455:Peptides; D040301:Vascular Endothelial Growth Factor Receptor-2
15N labelled peptides; NMR spectroscopy; VEGF receptors; living cells; peptide-protein interaction