期刊
JOURNAL OF MEDICINAL CHEMISTRY
卷 54, 期 7, 页码 2196-2206出版社
AMER CHEMICAL SOC
DOI: 10.1021/jm2000135
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资金
- EPFL
- Swiss National Science Foundation (SNSF) [PZ00P2-121933/1]
- Swiss Confederation [C09.0027]
- Austrian Science Foundation [J2882-N19]
- SNSF [200021-125147/1]
The inhibition activity of a series of anticancer metal complexes based on platinum, ruthenium, and gold metal ions was evaluated on the zinc-finger protein PARP-1, either purified or directly on protein extracts from human breast cancer MCF7 cells. Information on the reactivity of the metal complexes with the PARP-1 zinc-finger domain was obtained by high-resolution ESI FT-ICR mass spectrometry. An excellent correlation between PARP-1 inhibition in protein extracts and the ability of the complexes to bind to the zinc-finger motif (in competition with zinc) was established. The results support a model whereby displacement of zinc from the PARP-1 zinc finger by other metal ions leads to decreased PARP-1 activity. In vitro combination studies of cisplatin with NAMI-A and RAPTA-T on different cancer cell lines (MCF7, A2780, and A2780cisR) showed that, in some cases, a synergistic effect is in operation.
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