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  • DNA binding ability and hydrogen peroxide induced nuclease activity of a novel Cu(II) complex with malonate as the primary ligand and protonated 2-amino-4-picoline as the counterion.

DNA binding ability and hydrogen peroxide induced nuclease activity of a novel Cu(II) complex with malonate as the primary ligand and protonated 2-amino-4-picoline as the counterion.

The journal of physical chemistry. B (2010-04-13)
Biswarup Saha, Md Maidul Islam, Susmita Paul, Saheli Samanta, Shayoni Ray, Chitta Ranjan Santra, Somnath Ray Choudhury, Biswajit Dey, Amrita Das, Somnath Ghosh, Subrata Mukhopadhyay, Gopinatha Suresh Kumar, Parimal Karmakar
ABSTRACT

The DNA binding property of a Cu(II) complex, viz., [Cu(mal)(2)](picH)(2).2H(2)O, (mal)(2) = malonic acid, picH = protonated 2-amino-4-picoline, has been investigated in this study. The binding of this complex with plasmid and chromosomal DNA has been characterized by different biophysical techniques. From the absorption and fluorescence spectroscopic studies, it has been observed that the said copper complex binds strongly with pUC19 plasmid and CT DNA with a binding affinity of 2.368 x 10(3) and 4.0 x 10(3) M(-1), respectively, in 10 mM citrate-phosphate buffer, pH 7.4. Spectrofluorimetric studies reveal that the copper complex exhibits partial DNA intercalation as well as partial DNA minor groove binding properties. Consequently, in agarose gel electrophoresis study, it has been observed that the complex alone induces positive supercoiling in plasmid DNA while in the presence of H(2)O(2) it exhibits nuclease activity. The induction of the breakage in DNA backbone depends upon the relative concentrations of H(2)O(2) and copper complex followed by the time of incubation with DNA. Optical DNA melting study, isothermal titration calorimetry, and absorption spectroscopy have been used to characterize the nuclease activity of this complex in the presence of H(2)O(2). Further, (1)H NMR study indicates that Cu(II) in the complex is converted into the Cu(I) state by the reduction of H(2)O(2). Finally, agarose gel electrophoresis study with different radical scavengers concludes that the production of both hydroxyl radicals and reactive oxygen species is responsible for this nuclease activity.

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Sigma-Aldrich
2-Amino-4-methylpyridine, 99%