Abstract

Persistent organic pollutants (POPs) have been studied to accumulate in the food chain and detected in the boody of organisms such as amphibians. These pollutants are known to cause and promote growth of cancer. The details of POPs to cancer-linked protein interaction are essential for understanding the role in POPs toxicity. In this study, an in silico modeling was performed using homology modeling (SWISS-MODEL) and molecular docking (SwissDock) between the POPs (2,2',4,4',5,5'-Hexachlorobiphenyl (PCB153), 2,2',4,4'-Tetrabromodiphenyl ether (PBDE47) and 4,4'-Dichlorodiphenyl dichloroethylene (4,4'DDE)) and cancer-linked proteins (angiopoietin-related protein 7 (angptl7), annexin a2 (anxa2), SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin, subfamily A, member 2 (smarca2) and tumor protein (p53)) from western clawed frog (Xenopus tropicalis). The quality of the 3D models of angptl7, anxa2, p53 and smarca2 for X. tropicalis were assessed to verify the reliability and suitability for further molecular docking simulation using ERRAT and Molprobity. The molecular docking analysis revealed hydrophobic interactions of PCB153, PBDE47 and 4,4'DDE to binding pockets of all cancer-linked proteins. PCB153, PBDE47 and 4,4'DDE were bound to the same binding pocket in angptl7 and smarca2. Meanwhile, 4,4' DDE in anxa2 and p53 were bound to different binding pockets. PBDE47 had the highest binding energy in angptl7 (-6.98) and anxa2 (-7.32) while 4,4'DDE had the highest binding energy in p53 (-7.12) and smarca2 (-7.08). These in silico results showing POPs interacting directly with cancer-linked proteins via hydrophobic interaction may lead to alteration of the functions of cancer linked proteins involved in proliferation, invasion, and control of tumor cells.