Journal
JOURNAL OF INORGANIC BIOCHEMISTRY
Volume 144, Issue -, Pages 47-55Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2014.12.012
Keywords
Copper(II) compound; Human serum albumin; Cytotoxicity; Cell apoptosis
Funding
- Natural Science Foundation of China [31060121, 31460232, 21171043, 21431001]
- Natural Science Foundation of Guangxi [2012GXNSFCB053001, 2013GXNSFGA019010, 2014GXNSFDA118016]
- Technology division of Guilin [20130403-1]
- Guangxi 'Bagui' scholar program
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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.
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