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  • Title: Mutual influence of piceatannol and bisphenol F on their interaction with pepsin: Insights from spectroscopic, isothermal titration calorimetry and molecular modeling studies.
    Author: Shi Y, Liu M, Yan H, Cai C, Guo Q, Pei W, Zhang R, Wang Z, Han J.
    Journal: Spectrochim Acta A Mol Biomol Spectrosc; 2019 Jan 05; 206():384-395. PubMed ID: 30170174.
    Abstract:
    The individual and combined interactions of bisphenol F and piceatannol with pepsin were investigated using spectroscopic methods (fluorescence, UV-vis absorption, and circular dichroism spectroscopy), combined with isothermal titration calorimetry and molecular docking. Thermodynamic data showed that hydrogen bonds and van der Waals forces might play a major role for the binding process. Site marking experiments and molecular docking confirmed the binding sites of these two ligands on pepsin. The discrepancy in the binding constant between the binary and ternary systems indicated the competitive binding of piceatannol and bisphenol F to pepsin. Circular dichroism spectra studies suggested that the binding of the two ligands led to a loosening of pepsin backbone. Enzyme activity assays indicated that the inhibition of pepsin activity by piceatannol and bisphenol F was competitive. These results will be helpful to understand the mechanism of piceatannol and bisphenol F affecting the activity of digestive proteases in the sight of the food security.
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