2013
DOI: 10.1080/00958972.2013.827179
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Synthesis and structure of a new tetracopper(II) complex withN-benzoate-N′-[2-(2-hydroxyethylamino)ethyl]oxamide as bridging ligand:in vitroanticancer activities and DNA- and BSA-binding studies

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Cited by 21 publications
(4 citation statements)
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“…IC 50 values of 2 and 3 reach about 10 μM, lower than that of some previously reported analogous copper(II) complexes against these human alimentary system carcinoma cell lines [18][19][20][33][34][35][36], indicating that 2 and 3 have potent cytotoxicity.…”
Section: Copper(ii) Complexes 2353mentioning
confidence: 51%
“…IC 50 values of 2 and 3 reach about 10 μM, lower than that of some previously reported analogous copper(II) complexes against these human alimentary system carcinoma cell lines [18][19][20][33][34][35][36], indicating that 2 and 3 have potent cytotoxicity.…”
Section: Copper(ii) Complexes 2353mentioning
confidence: 51%
“…We also compared the DNA-binding properties of 1 with those of previously reported polycopper(II) complexes with various bridging ligands and polypyridines as terminal ligands [48][49][50][51], and we find that not only the interaction modes but also the DNA-binding ability of these polycopper(II) complexes are different, suggesting that interactions of these complexes toward DNA may be tuned by changing the bridging or terminal ligands. Such strategy should be valuable in designing new polynuclear complex systems and understanding the binding between these polynuclear complexes and DNA.…”
Section: Dna Interaction Studiesmentioning
confidence: 96%
“…It is sometimes very important to study the interaction of a bioactive compound with proteins, to gain fundamental insights of the binding mechanism and to understand the metabolism and transporting process of a drug compound. Therefore, to understand the protein binding activities of the cluster compound 10, BSA was used to study the tryptophan emissionquenching experiment [34]. Generally, the fluorescence of BSA is caused by three intrinsic characteristics of the protein, namely tryptophan, tyrosine and phenylalanine.…”
Section: Bsa Protein Binding Studiesmentioning
confidence: 99%