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Activation of Platinum(IV) Prodrugs by Cytochrome c and Characterization of the Protein Binding Sites
A. Lasorsa, O. Stuchlíková, V. Brabec, G. Natile, F. Arnesano,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Cisplatin chemistry metabolism MeSH
- Cytochromes c chemistry metabolism MeSH
- Mass Spectrometry MeSH
- Magnetic Resonance Spectroscopy MeSH
- Molecular Structure MeSH
- NAD chemistry metabolism MeSH
- Platinum chemistry metabolism MeSH
- Prodrugs chemistry metabolism MeSH
- Antineoplastic Agents chemistry metabolism MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Chromatography, High Pressure Liquid MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Platinum(IV) complexes generally require reduction to reactive Pt(II) species to exert their chemotherapeutic activity. The process of reductive activation of (15)N-labeled (OC-6-43)-bis(acetato)diamminedichloridoplatinum(IV), in the presence of nicotinamide adenine dinucleotide (NADH) and horse heart cytochrome c (cyt c), was monitored by (1)H,(15)N-HSQC NMR spectroscopy and protein digestion experiments. It has been shown that cyt c plays a catalytic role in the transfer of two reducing equivalents from NADH to Pt(IV) species. Noncovalent interactions between reduced monoaqua cisplatin (cis-[PtCl((15)NH3)2(H2O)](+)) and the protein, in the proximity of the heme cofactor, and also covalent binding of platinum to the protein region around Met65 and Met80 take place.
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- $a Lasorsa, Alessia $u Department of Chemistry, University of Bari "A. Moro" , via E. Orabona, 4, 70125 Bari, Italy.
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- $a Platinum(IV) complexes generally require reduction to reactive Pt(II) species to exert their chemotherapeutic activity. The process of reductive activation of (15)N-labeled (OC-6-43)-bis(acetato)diamminedichloridoplatinum(IV), in the presence of nicotinamide adenine dinucleotide (NADH) and horse heart cytochrome c (cyt c), was monitored by (1)H,(15)N-HSQC NMR spectroscopy and protein digestion experiments. It has been shown that cyt c plays a catalytic role in the transfer of two reducing equivalents from NADH to Pt(IV) species. Noncovalent interactions between reduced monoaqua cisplatin (cis-[PtCl((15)NH3)2(H2O)](+)) and the protein, in the proximity of the heme cofactor, and also covalent binding of platinum to the protein region around Met65 and Met80 take place.
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