期刊
CHEMOSPHERE
卷 220, 期 -, 页码 930-936出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.chemosphere.2018.12.194
关键词
Bisphenol A; Bisphenol A 3,4-quinone; Hemoglobin; Human serum albumin; Cytochrome c
资金
- national Natural Science Foundation of China [21505111, 21507106]
- General Research Fund from Research Grants Council (RGC) of Hong Kong, China [12301915]
- Nature Science Foundation of Hubei Province [4115/00051]
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.
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