The study on the interaction of Epigallocatechin gallate with bovine serum Albumin
DOI:
https://doi.org/10.5564/pmas.v59i4.1290Keywords:
Chromatographic method, binding parameter, fluorescence, thermodynamic parameterAbstract
In this study, we investigated the interaction of epigallocatechin gallate (EGCG) with bovine serum albumin (BSA) by fluorescence method and protein‐ligand docking. We separated EGCG from green tea using the chromatographic method and analyzed structural activity relationships of the EGCG. The results show that EGCG is a strong quencher of BSA fluorescence and binds with BSA with high affinity. The binding parameters (binding constant, the number of binding sites) were determined by the Ward equation. From the thermodynamic parameters, calculated according to the van’t Hoff equation, the enthalpy change ΔH°, and entropy change ΔS° were found to be -22.67 kJ/mol and 14.92 J/mol/K, respectively. These values suggest that apart from an initial hydrophobic association, the complex is held together by electrostatic and hydrogen bonding. In the docking simulation, the lowest free energies for the interaction of EGCG with tryptophan residues was −21.92kJ/mol (Trp134) and −24.7 kJ/mol (Trp213). The binding between EGCG and BSA consists of hydrogen bonds (Trp213) and hydrophobic interactions (Trp134).
Downloads
605
Downloads
Published
How to Cite
Issue
Section
License
Copyright on any research article in the Proceedings of the Mongolian Academy of Sciences is retained by the author(s).
The authors grant the Proceedings of the Mongolian Academy of Sciences a license to publish the article and identify itself as the original publisher.
Articles in the Proceedings of the Mongolian Academy of Sciences are Open Access articles published under a Creative Commons Attribution 4.0 International License CC BY.
This license permits use, distribution and reproduction in any medium, provided the original work is properly cited.