期刊
JOURNAL OF HAZARDOUS MATERIALS
卷 248, 期 -, 页码 313-321出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jhazmat.2012.12.056
关键词
Polychlorinated biphenyls (PCBs); Human serum albumin (HSA); Fluorescence; Molecular docking; Molecular dynamics
资金
- National Natural Science Foundation of China [31000017, 21207056]
- Natural Foundation of Gansu Province [1104WCGA187]
- Key Laboratory of Chemistry and Quality for Traditional Chinese Medicines of the College of Gansu Province [zzy-2011-03]
Polychlorinated biphenyls (PCBs) possessed much potential hazard to environment because of its chemical stability and biological toxicity. Here, we identified the binding mode of a representative compound, PCB153, to human serum albumin (HSA) using fluorescence and molecular dynamics simulation methods. The fluorescence study showed that the intrinsic fluorescence of HSA was quenched by addition of PCB153 through a static quenching mechanism. The thermodynamic analysis proved the binding behavior was mainly governed by hydrophobic force. Furthermore, as evidenced by site marker displacement experiments using two probe compounds, it revealed that PCB153 acted exactly on subdomain IIIA (site II) of HSA. On the other hand, the molecular dynamics studies as well as free energy calculations made another important contribution to understand the conformational changes of HSA and the stability of HSA-PCB153 system. Molecular docking revealed PCB153 can bind in a large hydrophobic activity of subdomain IIIA by the hydrophobic interaction and hydrogen bond interactions between chlorine atoms and residue ASN391. The present work provided reasonable models helping us further understand the transporting, distribution and toxicity effect of PCBs when it spread into human blood serum. Crown Copyright (C) 2013 Published by Elsevier B.V. All rights reserved.
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