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Synthesis, characterization and biological activities of homo-binuclear Cu(II) and Zn(II) complexes derived from 2-hydroxy-5-methyl-1,3-benzenedicarboxaldehyde derivatives

100%
Raman N., Sakthivel A., Jeyamurugan R.
Open Chemistry
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2010
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vol. 8
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issue 1
96-107
EN
Few novel binuclear Schiff base metal complexes [M2LCl3], where M = Cu(II) and Zn(II); L= 2,6-bis-({2-[(3-hydroxy-4-nitrobenzylidene)amino]ethylimino}methyl)-4-methylphenol (BHEM), 2,6-bis-({2-[(3,4-dimethoxybenzylidene)amino]ethylimino} methyl)-4-methylphenol (BDEM) and 2,6-bis-({2-[(2,3,5-trichlorobenzylidene)amino]ethylimino}methyl)-4-methylphenol (BTEM), have been synthesized and characterized by analytical and spectral data. The data suggest that BHEM/BDEM/BTEM ligands afford square-pyramidal/distorted square-pyramidal geometry on metalation with Zn(II)/Cu(II). The binding behaviour of these complexes with DNA has been investigated using electronic absorption spectroscopy as well as viscosity and voltammetric measurements; the results show that they interact with DNA through intercalating way. From the DNA cleavage study of these complexes, investigated by gel electrophoresis, we found that they efficiently cleave supercoiled pUC19 DNA in the presence of a reducing agent (3-mercaptopropionic acid) and on irradiation with UV light of 360 nm wavelength. The mechanism reveals that singlet oxygen (1O2) plays a significant role in the photo cleavage. The superoxide dismutase (SOD) mimetic activity of the synthesized complexes demonstrates that most of the complexes have promising SOD-mimetic activity. The antimicrobial study indicates that the complexes inhibit the growth of bacteria and fungi more than the free ligands. [...]
2
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Organoruthenium(II) thiosemicarbazone complexes: synthesis, spectral characterization, DNA binding and DNA cleavage studies

100%
Raja G., Jayabalakrishnan C.
Open Chemistry
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2013
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vol. 11
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issue 6
1010-1018
EN
A series of new ruthenium(II) complexes were synthesized with Schiff bases derived from salicylaldehyde / o-hydroxyacetophenone/ o-vanillin / 2-hydroxy-1-naphthaldehyde with thiosemicarbazide and acetyl furan. They are characterized by elemental analysis, IR, electronic, 1H NMR, 13C NMR and mass spectral studies. The elemental analysis suggests the stoichiometry to be 1:1 (metal:ligand). Four of these complexes were tested for its binding with CT-DNA using absorption spectroscopic studies and two of these complexes exhibit efficient DNA cleavage activity. [...]
3
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Synthesis, DNA-binding and antiproliferative activity of N-(Nitrogen heterocyclic) norcantharidin acylamide acid

88%
Zhu W.-Z., Hu R.-D., Lin Q.-Y., Wang X.-X., Zheng X.-L.
Open Chemistry
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2009
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vol. 7
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issue 3
569-575
EN
Two novel norcantharidin acylamide acids (HL1=N-pyrimidine norcantharidin acylamide acid, C12H13N3O4; HL2=N-pyridine norcantharidin acylamide acid, C13H14N2O4) were synthesized by a reaction of norcantharidin(NCTD) with 2-aminopyrimidine and 2-aminopyridine, respectively. Their structures were characterized by elemental analysis, IR, UV and 1 H NMR. Fluorescence titration and viscosity measurements indicated that HL1, HL2 and HL3 (HL3=N-phenyl norcantharidin acylamide acid, C14H15NO4) can bind calf thymus DNA via partial intercalation. The liner Stern-Volmer quenching constant Ksv values for HL1, HL2 and HL3 were 2.05 × 104 L mol−1, 1.15 × 104 L mol−1 and 8.30×103 L mol−1, respectively. Two compounds containing heterocycle of HL1 and HL2 have been found to cleave pBR322 plasmid DNA at physiological pH and temperature. The test of antiproliferation activity showed that the compounds had moderate to strong antiproliferative ability against the tested cell lines except of HL3 against the SMMC7721 cell line. The results indicated that the heterocycle attached to the norcantharidin was favorable to antiproliferative activity. This result was consistent with the DNA binding experiment. [...]
4
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In vitro DNA binding of purified CcpA protein from Lactococcus lactis IL1403

88%
Kowalczyk M., Borcz B., Płochocka D., Bardowski J.
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2007
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vol. 54
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issue 1
71-78
EN
During this study His-tagged CcpA protein purified under native conditions to obtain a biologically active protein was used for molecular analysis of CcpA-dependent regulation. Using electrophoretic mobility shift assays it was demonstrated that CcpA of L. lactis can bind DNA in the absence of the HPr-Ser-P corepressor and exhibits DNA-binding affinity for nucleotide sequences lacking cre sites. However, purified HPr-Ser-P protein from Bacillus subtilis was shown to slightly increase the DNA-binding capacity of the CcpA protein. It was also observed that CcpA bound to the cre box forms an apparently more stable complex than that resulting from unspecific binding. Competition gel retardation assay performed on DNA sequences from two PEP:PTS regions demonstrated that the ybhE, bglS, rheB, yebE, ptcB and yecA genes situated in these regions are most probably directly regulated by CcpA.
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