Inhibition of hydroxylated polychlorinated biphenyls (OH-PCBs) on sulfotransferases (SULTs).

Polychlorinated biphenyls (PCBs) have been demonstrated as a kind of the persistent organic pollutants (POPs) that could exert complicated influences towards metabolism in human bodies. Since hydroxylated polychlorinated biphenyls (OH-PCBs) are important metabolites of PCBs, our study focuses on investigating the potential inhibitory capability of OH-PCBs on four human sulfotransferase (SULT) isoforms. P-nitrophenol (PNP) was utilized as nonselective probe substrate for this study, and recombinant SULT isoforms were utilized as the enzyme resources. Ultra-performance liquid chromatography (UPLC)-UV detecting system was used to analyze PNP and its metabolite PNP-sulfate. As result, 100 μM of most tested OH-PCBs significantly inhibited the activity of four SULT isoforms. Concentration-dependent inhibition of OH-PCBs towards SULTs was found, and half inhibition concentration values (IC) of some inhibition processes were determined. Inhibition kinetics (inhibition kinetic type and parameters) were determined using 4'-OH-PCB106 as the representative OH-PCB, SULT1B1 and SULT1E1 as representative SULT isoforms. The inhibition kinetic parameters (K) were 1.73 μM and 1.81 μM for the inhibition of 4'-OH-PCB106 towards SULT1B1 and SULT1E1, respectively. In silico docking simulation was utilized to analyze the inhibition capability of 2'-OH-PCB5, 4'-OH-PCB9, 2'-OH-PCB12 towards SULT1A3.All these results obtained in this study are helpful for further understanding the toxicity of PCBs.