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Ni(II), Cu(II), and Zn(II) diethyldithiocarbamate complexes show various activities against the proteasome in breast cancer cells.

ABSTRACT: A series of three complexes with diethyldithiocarbamate ligand and three different metals (Ni, Cu, Zn) was prepared, confirmed by X-ray crystallography, and tested in human breast cancer MDA-MB-231 cells. Zinc and copper complexes, but not nickel complex, were found to be more active against cellular 26S proteasome than against purified 20S proteasome core particle. One of the possible explanations is inhibition of JAMM domain in the 19S proteasome lid.

SUBMITTER: Cvek B

PROVIDER: S-EPMC2574941 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature

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Ni(II), Cu(II), and Zn(II) diethyldithiocarbamate complexes show various activities against the proteasome in breast cancer cells.

Cvek Boris B Milacic Vesna V Taraba Jan J Dou Q Ping QP

Journal of medicinal chemistry 20080925 20

A series of three complexes with diethyldithiocarbamate ligand and three different metals (Ni, Cu, Zn) was prepared, confirmed by X-ray crystallography, and tested in human breast cancer MDA-MB-231 cells. Zinc and copper complexes, but not nickel complex, were found to be more active against cellular 26S proteasome than against purified 20S proteasome core particle. One of the possible explanations is inhibition of JAMM domain in the 19S proteasome lid. ...[more]

PMID: 18816109

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Project description:New Schiff base ligand, derived from antiviral valacyclovir, and its novel Cr(III), Mn(II), Co(II), Ni(II), Cu(II), Zn(II) complexes have been synthesized. By using a variety of analytical and spectroscopic techniques, the type of bonding between the ligand and the metal ions in the recently formed complexes was clarified. The Schiff base ligand act as a bidentate and coordinated with the metal ions through the azomethine-N and the phenolic-O centers, in a mono-deprotonated form. Except for the Zn(II) complex, which displayed a tetrahedral geometry, all complexes displayed octahedral geometry. The TGA findings supported that the stability and decomposition properties of the metal complexes were entirely distinct from one another. The thermogram showed decomposition of all investigated metal complexes above 200 °C in three, four or five steps, and indicated the high thermal stability of these complexes. According to XRD patterns, the particles of these complexes were located at the nanoscale. Moreover, for all the samples analyzed, the TEM images showed uniform and homogeneous surface morphology. The biological activity revealing the high efficiencies of the screened complexes as antibacterial and antitumor agents. The antimicrobial activity of the ligand and its complexes was examined against a variety of pathogenic bacteria and fungi including Escherichia coli, Staphylococcus aureus and Candida albicans. The data obtained revealed that the metal ion in the complexes enhanced the antimicrobial activity compared to the free ligand. The high efficiencies toward S. aureus, E. coli, and C. albicans appeared by Cu(II) complex 23, Ni(II) complex 20, and Ni(II) complex 19, respectively. The antitumor activity of the ligand and its complexes was tested against Hepatocellular carcinoma cell line (HepG-2 cells), the residue 28 which produced after heating the Cu(II) complex 25 at 200 °C for 1 h, exhibited strong inhibition of HepG-2 cell growth. The results of the DNA cleavage investigation demonstrated the ability of investigated Cu(II) complex to degrade DNA. The docking findings showed strong interactions of both the ligand and its examined Cu(II) complex, revealing their ability to cleavage DNA and their potent inhibitory effects on tumor cells. The electrical conductivity study confirmed that the ligand and its investigated complexes had semiconducting properties.

Dataset Information

Ni(II), Cu(II), and Zn(II) diethyldithiocarbamate complexes show various activities against the proteasome in breast cancer cells.

Publications

Ni(II), Cu(II), and Zn(II) diethyldithiocarbamate complexes show various activities against the proteasome in breast cancer cells.

Similar Datasets

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