Abstract
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.
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