Journal
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
Volume 206, Issue -, Pages 384-395Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2018.08.028
Keywords
Bisphenol F; Piceatannol; Fluorescence spectroscopy; Circular dichroism; Isothermal titration calorimetry; Molecular modeling
Categories
Funding
- National Natural Science Foundation of China [21473085]
- Key Research and Development Program of Shandong Province of China [2015GSF118160]
- Open Project of Shandong Collaborative Innovation Center for Antibody Drugs [CIC-AD1832]
- Tai-Shan Scholar Research Fund of Shandong Province of China [319190201]
Ask authors/readers for more resources
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. (C) 2018 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available