Interaction of bisphenol A 3, 4-quinone metabolite with human hemoglobin, human serum albumin and cytochrome c in vitro

Since covalent protein-bisphenol A adducts generated by the interaction of protein nucleophiles with bisphenol A quinone affect the physicochemical properties of proteins in functional foods and biological tissues, it has become a hot topic nowadays. Therefore, we investigated the interaction of several different biomacromolecules such as hemoglobin, human serum albumin and cytochrome c with bisphenol A 3, 4-quinone (BPAQ). The effects of binding on changes in biomolecular structure were determined by various spectroscopic methods. BPAQ effects were investigated by using the UV-Vis spectroscopy and the quenching phenomenon from fluorescence emission. It proved that the formation of bio-complex and their aromatic micro-environment was likely to be disturbed with as well. Changes observed in circular dichroism (CD) spectroscopy confirmed the quantitative loss of the alpha helical structure. Further studies with matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOFMS) and molecular docking indicated combining ratio and binding sites between proteins and BPAQ The in vitro data of BPAQ-proteins adducts may provide a valuable theoretical basis for the elucidation of the toxicological mechanisms of BPAQ adducts in biological systems and environments. (C) 2019 Elsevier Ltd. All rights reserved.