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  • Title: An investigation into the altered binding mode of green tea polyphenols with human serum albumin on complexation with copper.
    Author: Singha Roy A, Ghosh KS, Dasgupta S.
    Journal: J Biomol Struct Dyn; 2013 Oct; 31(10):1191-206. PubMed ID: 23145958.
    Abstract:
    Green tea is rich in several polyphenols, such as (-)-epicatechin-3-gallate (ECG), (-)-epigallocatechin (EGC), and (-)-epigallocatechin-3-gallate (EGCG). The biological importance of these polyphenols led us to study the major polyphenol EGCG with human serum albumin (HSA) in an earlier study. In this report, we have compared the binding of ECG, EGC, and EGCG and the Cu(II) complexes of EGCG and ECG with HSA. We observe that the gallate moiety of the polyphenols plays a crucial role in determining the mode of interaction with HSA. The binding constants obtained for the different systems are 5.86 ± 0.72 × 10⁴ M⁻¹ (K ECG-HSA), 4.22 ± 0.15 × 10⁴ M⁻¹ (K ECG-Cu(II)-HSA), and 9.51 ± 0.31 × 10⁴ M⁻¹ (K EGCG-Cu(II)-HSA) at 293 K. Thermodynamic parameters thus obtained suggest that apart from an initial hydrophobic association, van der Waals interactions and hydrogen bonding are the major interactions which held together the polyphenols and HSA. However, thermodynamic parameters obtained from the interactions of the copper complexes with HSA are indicative of the involvement of the hydrophobic forces. Circular dichroism and the Fourier transform infrared spectroscopic measurements reveal changes in α-helical content of HSA after binding with the ligands. Data obtained by fluorescence spectroscopy, displacement experiments along with the docking studies suggested that the ligands bind to the residues located in site 1 (subdomains IIA), whereas EGC, that lacks the gallate moiety, binds to the other hydrophobic site 2 (subdomain IIIA) of the protein.
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