Enhancing the copper(II) complexes cytotoxicity to cancer cells through bound to human serum albumin
Enhancing the copper(II) complexes cytotoxicity to cancer cells through bound to human serum albumin
复制标题
通过与人血清白蛋白结合，增强铜 (II) 复合物对癌细胞的细胞毒性。
DOI：
10.1016/j.jinorgbio.2014.12.012
复制
发表时间：
2015-03-01
影响因子：
3.9
通讯作者：
Liang, Hong
中科院分区：
文献类型：
--
作者：
Gou, Yi;Zhang, Yao;Liang, Hong
We use Schiff-base salicylaldehyde benzoylhydrazone (HL) as the ligand for copper(II), resulting in the complexes [CuCl(L)]center dot H2O (C1), [CuNO3(L)]center dot H2O (C2) and [CuBr(L)](2) (C3). We characterize the Cu(II) compounds' interactions with human serum albumin (HSA) using fluorescence spectroscopy and molecular docking. These studies revealed that Cu(II) compounds propensity bound to IIA subdomain of HSA possible by hydrophobic interactions and hydrogen bond. Cu(II) compounds produce intracellular reactive oxygen species (ROS) in cancer cells. Complexes of HSA and copper(II) compounds enhance about 2-fold cytotoxicity in cancer cells but do not raise cytotoxicity levels in normal cells in vitro. Compared with C3 alone, HSA-C3 complex promotes HepG2 cell apoptosis and has a stronger capacity to promote cell cycle arrest at the G2/M phase of HepG2. (C) 2014 Elsevier Inc. All rights reserved.
