The study on the interaction of Epigallocatechin gallate with bovine serum Albumin
Keywords:Chromatographic method, binding parameter, fluorescence, thermodynamic parameter
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).
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