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• W2767937367 abstract "A copper(II) complex [CuII(quamol)Cl]·H2O, where H(quamol) is N-2-(quinolyl-methylidene)aminophenol, has been isolated. The solution structure of the complex has been assessed to be distorted square-planar. The complex displays a ligand field band in the visible region (608 nm) and also show axial EPR spectrum in DMF at 77 K with g|| > g⊥ indicating a dx2-y2 ground state. The g|| and A|| values of 2.265 and 153 × 10−4 cm−1, respectively, conform to a square-based CuN2OCl chromophore. The interaction of the complex with calf thymus (CT) DNA has been explored by using absorption (Kb = 2.48 × 105 M−1), emission (Kapp = 7.72 × 104 M−1) and circular dichroic (CD) spectral measurements, which reveals that a complex interacts strongly with DNA through partial intercalation. The electrochemical studies indicate that Cu(II) binds to DNA more strongly than Cu(I). It cleaves ϕX174 supercoiled phage DNA in the presence of ascorbic acid as a reducing agent. Meanwhile, the interaction of the complex with bovine serum albumin (BSA) indicates that the complex can markedly quench the intrinsic fluorescence of BSA via a static quenching process and cause its conformational change. Interestingly, the observed IC50 values for the cell lines EVSA-T (breast cancer) and M19 MEL (melanoma) are in the range of those observed with cisplatin while M19 MEL cancer cell line, complex is more active than 5-fluorouracil. The complex is non-toxic to healthy cells." @default.
• W2767937367 created "2017-11-17" @default.
• W2767937367 creator A5001416845 @default.
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• W2767937367 date "2018-02-01" @default.
• W2767937367 modified "2023-10-17" @default.
• W2767937367 title "Non-covalent DNA binding, protein interaction, DNA cleavage and cytotoxicity of [Cu(quamol)Cl]·H2O" @default.
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• W2767937367 doi "https://doi.org/10.1016/j.ijbiomac.2017.10.131" @default.
• W2767937367 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29104051" @default.
• W2767937367 hasPublicationYear "2018" @default.
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