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. 2018 Oct 11;13(10):e0204856.
doi: 10.1371/journal.pone.0204856. eCollection 2018.

Thermodynamic and computational analyses reveal the functional roles of the galloyl group of tea catechins in molecular recognition

Tomoya Takahashi  1   2 , Satoru Nagatoishi  1   3 , Daisuke Kuroda  1   4 , Kouhei Tsumoto  1   3   4
Affiliations

Thermodynamic and computational analyses reveal the functional roles of the galloyl group of tea catechins in molecular recognition

Tomoya Takahashi et al. PLoS One. .

Abstract

Catechins, biologically active polyphenols in green tea, exhibit various biological activities, such as anticancer and antiviral activities, arising from interactions with functional proteins. However, the molecular details of these interactions remain unclear. In this study, we investigated the interactions between human serum albumin (HSA) and various catechins, including some with a galloyl group, by means of isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC), and docking simulations. Our results indicate that the galloyl group was important for recognition by HSA and was responsible for enthalpic gains derived from a larger buried surface area and more van der Waals contacts. Thus, our thermodynamic and computational analyses suggest that the galloyl group plays important functional roles in the specific binding of catechins to proteins, implying that the biological activities of these compounds may be due in part to the physicochemical characteristics of the galloyl group.

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Conflict of interest statement

The Kao Corporation provided support in the form of salaries for author TT. This does not alter our adherence to PLOS ONE policies on sharing data and materials.

Figures

Fig 1
Fig 1. Chemical structures of catechins.
(A) Chemical structure of the functional groups in catechins, (B) natural epicatechins (top row) and synthetic catechins (bottom row), and (C) ethyl gallate and analogs of the galloyl group and catechinsepigallocatechin gallate.
Fig 2
Fig 2. Correlation between ΔG in vitro and interface score in silico for binding of catechins and ethyl gallate to human serum albumin.
Fig 3
Fig 3
Correlations between buried surface area (BSA), shape complementarity (Sc), and ΔG for catechins and ethyl gallate: (A) plot of ΔG versus BSA and (B) plot of ΔG versus Sc.
Fig 4
Fig 4. Model of a complex between human serum albumin (white) and (−)-epigallocatechin gallate (black) obtained by means of a docking simulation.
Only residues that formed hydrogen bonds with EGCg were shown. Hydrogen bonds were described as cyan dotted lines. The molecular surface of the protein was colored based on the Kyte–Doolittle hydrophobicity scale (blue for hydrophilic areas and red for hydrophobic areas [38]). The figure was made by the UCSF Chimera [46].
See this image and copyright information in PMC

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