Abstract:
BACKGROUND:Polychlorinated biphenyls (PCBs) are ubiquitous environment-contaminating synthetic chemicals that have been associated with increased risk of hepatic cancer, melanoma, non-Hodgkin lymphoma and cancer of many other body organs. Structural binding analyses of PCB 77 and PCB 118 with peroxisome proliferator-activated receptors (PPARα, PPARβ/δ and PPARγ) was performed to predict the association of PCBs with potential disruption of PPAR signaling pathways. MATERIALS AND METHODS:The crystal structures of human PPARα, PPARβ/δ and PPARγ were obtained from the Protein Data Bank. Structures of PCB 77 and PCB 118 were obtained from PubChem database. Docking was performed using glide (Schrodinger) induced fit docking (IFD) module. RESULTS:The PCB 77 and PCB 118 interacted with PPARα, PPARβ/δ and PPARγ showing an overlapping of 40-58% interacting amino acid residues with synthetic co-complex agonists of the three PPARs. The binding affinity was higher for PCB 118 than for PCB 77 during docking interactions with each of the three PPARs. CONCLUSION:The consistent commonality of interacting residues for PCB 77 and PCB 118 with co-complex synthetic agonists of the PPARs together with good binding affinity suggested that the PPAR signaling pathway is a potential target for toxicologic activity of PCBs.
journal_name
Anticancer Resjournal_title
Anticancer researchauthors
Sheikh IA,Khweek AA,Beg MAdoi
10.21873/anticanres.11202subject
Has Abstractpub_date
2016-11-01 00:00:00pages
6117-6124issue
11eissn
0250-7005issn
1791-7530pii
36/11/6117journal_volume
36pub_type
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journal_title:Anticancer research
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journal_title:Anticancer research
pub_type: 杂志文章
doi:
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doi:
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doi:
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doi:
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