Abstract
As an endocrine-disrupting chemical, bisphenol A (BPA), can affect normal endocrine function of hormone. This paper studied the toxic effect of BPA on acid phosphatase at the molecular level by multi-spectroscopic measurements, molecular docking, and enzyme activity experiment. BPA could enhance the fluorescence intensity, change the structure, and cause an increased hydrophobicity of acid phosphatase. Hydrogen bond interaction and van der Waals forces were the main forces to generate the BPA-acid phosphatase complex on account of the negative ΔH (− 36.92 kJ mol−1) and ΔS (− 50.78 J mol−1 K−1). BPA led to the loosening and unfolding of protein structure and extending the peptide strands, as revealed by UV-vis absorption and CD spectra. Based on the enzyme activity experiment, BPA could decrease the activity of the acid phosphatase by entering the active site of the enzyme. The molecular docking model showed that BPA could bind into the cavity of acid phosphatase and interact with Tyr A252 and a hydrogen bond (1.47 Å) was formed in the binding process. This work suggested the structures and functions of acid phosphatase were both affected by BPA.
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Acknowledgements
This work is co-supported by NSFC (21277081, 21477067, and 21507071), the Cultivation Fund of the Key Scientific and Technical Innovation Project, Research Fund for the Doctoral Program of Higher Education and Ministry of Education of China (20130131110016), and Science and Technology Development Plan of Shandong Province (2014GSF117027). The Fundamental Research Funds of Shandong University (2014BT013, 2015JC010 and 2015JC030) are also acknowledged.
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Xu, M., Zhang, R., Song, W. et al. Probing the toxic mechanism of bisphenol A with acid phosphatase at the molecular level. Environ Sci Pollut Res 25, 11431–11439 (2018). https://doi.org/10.1007/s11356-018-1378-7
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DOI: https://doi.org/10.1007/s11356-018-1378-7