Exploring the toxic interactions between Bisphenol A and glutathione peroxidase 6 from Arabidopsis thaliana

As primary industrial raw material, the widespread usage of bisphenol A (BPA) has resulted in sustained release and accumulation in the environment. Besides its endocrine-disrupting character, BPA was reported to generate excessive reactive oxygen species (ROS). However, the potential toxic mechanisms of the BPA-induced oxidative damage to plants were poorly understood. In this study, glutathione peroxidase 6 from Arabidopsis thaliana (AtGPX6) was regarded as biomarker to investigate the toxic effects of BPA on plants by multi-spectroscopic techniques and molecular docking method. Firstly, BPA effectively quenched the intrinsic fluorescence of AtGPX6 via static quenching mechanism, and a single binding site of AtGPX6 towards BPA was presumed. Moreover, the binding force was mainly driven by van der Waals forces and hydrogen bonding based on the negative values of ΔH⁰ and ΔS⁰, which was consistent with the molecular docking result. In addition, the conformational changes of AtGPX6 accompanied with the enhancement of the hydrophilicity around the tryptophan residues upon the combination with BPA, were evaluated through the combination of the fluorescence, UV-visible absorption and Circular dichroism (CD) spectroscopy. Finally, the inhibitory impact on the development of Arabidopsis seedling roots was observed under BPA exposure. Therefore, the exploration of the molecular mechanism of AtGPX6 with BPA would provide valuable assessments on the toxic effects of BPA on plants.