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Personal Style
Apparel
Skin
Scene
Measurements
Length
14.27 m
Wingspan
14.91 m
Weight
11011.75 kg
Genetics
Cream
Basic
Basic
Cornflower
Basic
Basic
Sunset
Basic
Basic
Hatchday
Breed
Eye Type
Level 1 Guardian
EXP: 0 / 245
STR
7
AGI
6
DEF
8
QCK
5
INT
5
VIT
8
MND
6
Biography
https://www.researchgate.net/publication/309568468_Peroxisome_Proliferator-activated_Receptors_as_Potential_Targets_for_Carcinogenic_Activity_of_Polychlorinated_Biphenyls_A_Computational_Perspective
Peroxisome Proliferator-activated Receptors as Potential Targets for Carcinogenic Activity of Polychlorinated Biphenyls: A Computational Perspective
Article in Anticancer research 36(11):6117-6124 · November 2016 with 8 Reads
DOI: 10.21873/anticanres.11202
Cite this publication
Ishfaq Sheikh
28.23King Abdulaziz University
ARWA ABU KHWEEK
Mohd Amin Beg
41.65King Abdulaziz University
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.
Peroxisome Proliferator-activated Receptors as Potential Targets for Carcinogenic Activity of Polychlorinated Biphenyls: A Computational Perspective
Article in Anticancer research 36(11):6117-6124 · November 2016 with 8 Reads
DOI: 10.21873/anticanres.11202
Cite this publication
Ishfaq Sheikh
28.23King Abdulaziz University
ARWA ABU KHWEEK
Mohd Amin Beg
41.65King Abdulaziz University
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.
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