Metal-Based Inhibition of Poly(ADP-ribose) Polymerase - The Guardian Angel of DNA

被引：127

作者：

Mendes, Filipa ^{[2
]}

Groessl, Michael ^{[1
]}

Nazarov, Alexey A. ^{[1
]}

Tsybin, Yury O. ^{[1
]}

Sava, Gianni ^{[3
]}

Santos, Isabel ^{[2
]}

Dyson, Paul J. ^{[1
]}

Casini, Angela ^{[1
]}

机构：

[1] Ecole Polytech Fed Lausanne, Inst Sci & Ingn Chim, CH-1015 Lausanne, Switzerland

[2] Inst Tecnol & Nucl, Unidade Ciencias Quim & Radiofarmaceut, P-2686953 Sacavem, Portugal

[3] Callerio Fdn Onlus, I-34127 Trieste, Italy

来源：

JOURNAL OF MEDICINAL CHEMISTRY | 2011年 / 54卷 / 07期

基金：

瑞士国家科学基金会;

关键词：

SOLUTION CHEMISTRY; NUCLEAR PROTEINS; ZINC FINGERS; ANTICANCER METALLODRUGS; GOLD(III) COMPLEXES; MASS-SPECTROMETRY; ESCHERICHIA-COLI; CATHEPSIN-B; IN-VITRO; NAMI-A;

D O I：

10.1021/jm2000135

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

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.

引用

页码：2196 / 2206

页数：11

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