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

Tomoya Takahashi; Satoru Nagatoishi; Daisuke Kuroda; Kouhei Tsumoto

doi:10.1371/journal.pone.0204856

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

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

Authors

Tomoya Takahashi^{1

2}, Satoru Nagatoishi^{1

3}, Daisuke Kuroda^{1

4}, Kouhei Tsumoto^{1

3

4}

Affiliations

¹ Department of Bioengineering, School of Engineering, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan.
² Global R&D, Health Care Food, Kao Corporation, Bunka, Sumida-ku, Tokyo, Japan.
³ Institute of Medical Science, The University of Tokyo, Shirokanedai, Minato-ku, Tokyo, Japan.
⁴ Medical Device Development and Regulation Research Center, School of Engineering, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan.

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Binding Sites
Calorimetry, Differential Scanning
Catechin / chemistry*
Catechin / pharmacology*
Humans
Models, Molecular
Molecular Docking Simulation
Molecular Structure
Plant Extracts / chemistry
Plant Extracts / pharmacology
Protein Binding
Serum Albumin, Human / chemistry*
Serum Albumin, Human / metabolism*
Structure-Activity Relationship
Tea / chemistry*
Thermodynamics

Substances

Plant Extracts
Tea
Catechin
Serum Albumin, Human

Grants and funding

The Kao Corporation provided support in the form of salaries for author TT, but did not have any additional role in the study design, data collection and analysis, decision to publish, or preparation of the manuscript. The specific roles of these authors are articulated in the ‘author contributions’ section. Additionally, super-computing resources in this study were provided in part by the ROIS National Institute of Genetics, and by the Human Genome Center at the Institute of Medical Science, The University of Tokyo, Japan.