The combined effects of bisphenol S and hexavalent chromium on alpha-glucosidase: Intermolecular interaction, structural and functional changes

The co-contamination of heavy metal ions and organic pollutants has posed a threat to human health. Herein, this study investigated the intermolecular interactions of bisphenol S (BPS) and hexavalent chromium (Cr(VI)) under both individual and coexisting conditions, with alpha-glucosidase (AG), a key enzyme in carbohydrate metabolism, and the corresponding effects on the structure and function of AG. Multiple spectroscopic and molecular docking methods were employed to conduct the investigation in vitro and in silico. The results indicated that both BPS and Cr(VI) quenched the fluorescence of AG via a combined static and dynamic quenching processes. At 310 K, the binding constants of AG with BPS in the AG-BPS and (AG-Cr(VI))-BPS systems were 1.84 x 10(4) and 2.03 x 10(4) L mol(-1), and the binding constants of AG with Cr(VI) in the AG-Cr(VI) and (AG-BPS)-Cr(VI) systems were 6.14 x 10(3) and 4.35 x 10(3) L mol(-1). Cr(VI) could significantly affect the binding site of BPS in AG, while BPS had a minimal impact on the binding site of Cr(VI) in AG. BPS and Cr(VI) caused varied structural alterations of AG, and the impact of their coexistence on the structure of AG was related to the order in which they were added. Both BPS and Cr(VI) had a concentration-related effect on AG activity. This study provides valuable insights into the molecular mechanisms underlying the combined toxic effects of BPS and Cr(VI) on AG, highlighting the potential health risks associated with their environmental co-exposure.