Probing the toxic interactions between bisphenol A and glutathione S-transferase Phi8 from Arabidopsis thaliana

As primary polymer material in industrial products, bisphenol A (BPA) has become one of the most productive chemicals. Excluding its endocrine-disrupting property, BPA can also produce excessive reactive oxygen species (ROS). Nevertheless, the underlying toxic mechanisms of BPA-induced oxidative damages to plants are still unknown. In this work, glutathione S-transferase Phi8 was used as biomarker to evaluate the hazardous oxidative effects of BPA at the molecular level. Firstly, the intrinsic fluorescence of AtGSTF8 was statically quenched along with complex formation and structural and conformational changes, which led to the loosening and unfolding of the framework of AtGSTF8 as well as the increase of hydrophilicity around Trp residues. Then a single binding site was predicted for AtGSTF8 towards BPA and the complex formation was predominantly driven by hydrophobic interactions owing to the positive ΔH and ΔS. Besides, the predicted binding site of BPA was close to the H-site of AtGSTF8 which was surrounded by several hydrophobic amino acids based on the molecular docking results. The activity of glutathione S-transferase was declined and the plant growth was destroyed upon complex formation. The investigation of the binding mechanism of BPA with AtGSTF8 at molecular level would provide experimental assessments on toxicological effects of BPA on plants.