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VEGFR Recognition Interface of a Proangiogenic VEGF‐Mimetic Peptide Determined In Vitro and in the Presence of Endothelial Cells by NMR Spectroscopy
Author(s) -
Di Stasi Rossella,
Diana Donatella,
Capasso Domenica,
Di Gaetano Sonia,
De Rosa Lucia,
Celentano Veronica,
Isernia Carla,
Fattorusso Roberto,
D'Andrea Luca D.
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201802117
Subject(s) - peptide , vascular endothelial growth factor , receptor , context (archaeology) , in vitro , microbiology and biotechnology , vegf receptors , kinase insert domain receptor , chemistry , biology , vascular endothelial growth factor a , biophysics , biochemistry , cancer research , paleontology
QK peptide is a vascular endothelial growth factor (VEGF)‐mimetic molecule with significant proangiogenic activity. In particular, QK is able to bind and activate VEGF receptors (VEGFRs) to stimulate a functional response in endothelial cells. To characterize the peptide bioactivity and its molecular recognition properties, a detailed picture of the interaction between peptide QK and VEGF receptors is reported. By combining NMR spectroscopy studies in solution on the purified receptor and in the presence of intact endothelial cells, a molecular description of the binding interaction between peptide QK and VEGFR2 in the cellular context is obtained. These results reveal useful insights into the peptide biological mechanism, which opens the way to further optimization of this class of VEGF‐mimicking peptides.