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• W2503137435 abstract "Abstract Three oxovanadium complexes incorporating thiosemicarbazones and fluoro-phenanthroline derivatives [VO(hntdtsc)(CF3PIP)] (1) (hntdtsc = 2-hydroxyl-1-naphthaldehyde thiosemicarbazone, CF3PIP = 2-(2-trifluoromethyl phenyl)imidazole[4,5-f][1,10]phenanthroline [VO(hntdtsc)(m-CF3PIP)] (2) (m-CF3PIP = 2-(3-trifluoromethyl phenyl)imidazole[4,5-f][1,10]phenanthroline), [VO(hntdtsc)(p-CF3PIP)] (3) (p-CF3PIP = 2-(4-trifluoromethyl phenyl)imidazole[4,5-f][1,10]phenanthroline) were newly synthesized and characterized by elemental analysis and spectroscopic techniques. Their interactions with calf-thymus DNA (CT-DNA) and photocleavage properties with plasmid pBR322 DNA were investigated by a host of analytical methods. The results suggest that these three complexes interact with CT-DNA through an non-classical intercalative mode and can efficiently cleavage plasmid pBR322 DNA upon exposure to ultraviolet light. In addition, they all exhibited considerable anti-proliferative activity in vitro against human Hela, CaSki, SiHa, ECa9706, ECa109, MDA-MB-231 and MCF-7 tumor cell lines, to have an IC50 values for cytotoxicity in the low micromole range 0.31–6.15 μM, which is very close to that of cisplatin (0.52–2.49 μM). Furthermore, their antitumor mechanism has been analyzed by the cell cycle arrest, and apoptosis analysis. The results showed that complexes 2 and 3 caused G0/G1 phase arrest in ECa9706 cells, but differentiatedly induced G0/G1 and S phase arrest in ECa109 cells. And significant apoptosis were observed in both the two tumor cell lines, which indicate these oxovanadium complexes induce proliferative suppression of ECa9706 and ECa109 cells via the induction of apoptosis." @default.
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• W2503137435 date "2016-10-01" @default.
• W2503137435 modified "2023-10-16" @default.
• W2503137435 title "The anti-tumor activity of novel oxovanadium complexes derived from thiosemicarbazones and fluoro-phenanthroline derivatives" @default.
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• W2503137435 doi "https://doi.org/10.1016/j.poly.2016.07.021" @default.
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