Synthesis, characterization, DNA binding and cleavage, HSA interaction and cytotoxicity of a new copper(II) complex derived from 2-(2′-pyridyl)benzothiazole and glycylglycine

被引:69
作者
Fu, Xia-Bing [1 ]
Weng, Gui-Tian [1 ]
Liu, Dan-Dan [1 ]
Le, Xue-Yi [1 ,2 ]
机构
[1] South China Agri Univ, Dept Appl Chem, Guangzhou 510642, Guangdong, Peoples R China
[2] South China Agri Univ, Inst Biomat, Guangzhou 510642, Guangdong, Peoples R China
关键词
Copper(II)-dipeptide complex; 2-(2 '-Pyridyl)benzothiazole; DNA binding; Nuclease activity; HSA interaction; Cytotoxicity; BOVINE SERUM-ALBUMIN; ANTICANCER ACTIVITY; IN-VITRO; FLUORESCENCE; TRIS(PHENANTHROLINE)RUTHENIUM(II); DERIVATIVES; PEPTIDE; LIGAND; BENZOTHIAZOLE; OXORHENIUM(V);
D O I
10.1016/j.jphotochem.2013.12.002
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
A new copper(II) complex, [Cu(glygly)(pbt)(H2O)]CIO4 (glygly = glycylglycine anion and pbt =2-(2'-pyridyl)benzothiazole) was synthesized and characterized by elemental analysis, molar conductivity, mass spectra, IR spectra, UV-vis spectra and thermogravimetric analysis (TGA). Spectroscopic titration, viscosity, and electrophoresis measurements revealed that the complex intercalated to calf thymus (CT)-DNA with moderate binding affinity (K-b =5.64 x 10(4) M-1), and cleaved pBR322 DNA at a low concentration of 5 mu M in the presence of ascorbic acid, presumably via an oxidative mechanism. Further, the protein-binding ability has been monitored by various spectroscopic techniques (UV-vis, fluorescence and CD) using human serum albumin (HSA) as a model protein. The complex displayed desired affinity to HSA in which hydrophobic interaction played a major role. In addition, the complex was subjected to cytotoxicity tests in vitro using three human cancer cells lines (HepG2, HeLa and A549) and showed prominent and selective cytotoxicity against HepG2 cell lines (IC50 similar to 17.78 mu.M). (C) 2013 Elsevier B.V. All rights reserved.
引用
收藏
页码:83 / 95
页数:13
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