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- W2298034502 abstract "The vascular endothelial growth factor A (VEGF-A) is a potent angiogenic factor, its activity may be influenced by the presence of copper(II) ions. To mimic the interaction between copper(II) and VEGF (Vascular Endotelial Growth Factor), the N- and C-terminally blocked peptide fragments VEGF73-101 and VEGF84-101, owing to VEGF165 protein, have been synthesized. These protein domains represent a specific recognition site with the VEGF receptor (VEGFR). Copper(II) complexes with VEGF73-101 and VEGF84-101 were investigated by means of potentiometry and UV-Vis, ESI-MS, CD, EPR spectroscopic methods. Both peptides have three histidine residues and display a binding high affinity for copper(II) ions. The proliferative activity of the peptides in the absence and presence of copper(II) ions as well as of VEGF-165 protein was also tested on HUVEC cells (Human Umbilical Vein Endothelial Cells). The VEGF73-101 showed a dose-dependent anti-proliferative activity, while the shorter peptide VEGF84-101 did not affect HUVEC proliferation, both in the presence and in the absence of VEGF." @default.
- W2298034502 created "2016-06-24" @default.
- W2298034502 creator A5009190426 @default.
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- W2298034502 date "2016-06-01" @default.
- W2298034502 modified "2023-10-13" @default.
- W2298034502 title "The Inorganic Perspective of VEGF: Interactions of Cu2+ with Peptides Encompassing a Recognition Domain of the VEGF Receptor" @default.
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- W2298034502 doi "https://doi.org/10.1016/j.jinorgbio.2016.03.004" @default.
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