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Molecules 2018, 23(5), 1125; https://doi.org/10.3390/molecules23051125

Binding of Catechins to Staphylococcal Enterotoxin A

1
School of Food and Nutritional Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka 422-8526, Japan
2
Faculty of Nutrition, Kobe Gakuin University, 518 Arise, Ikawadani-cho, Nishi-ku, Kobe 651-2180, Japan
3
Department of Kampo Pharmacy, Yokohama University of Pharmacy, 601 Matano-cho, Totsuka-ku, Yokohama 245-0066, Japan
4
Department of Synthetic Organic & Medicinal Chemistry, School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka 422-8526, Japan
Present address: Department of Food Science and Nutrition, Nara Women’s University, Kita-Uoya Nishimachi, Nara 630-8506, Japan.
Present address: Department of Nutrition and Health Sciences, Faculty of Food and Nutritional Sciences, Toyo University 1-1-1 Izumino, Itakura-machi, Oura-gun, Gunma 374-0193, Japan.
*
Author to whom correspondence should be addressed.
Received: 19 April 2018 / Revised: 6 May 2018 / Accepted: 7 May 2018 / Published: 9 May 2018
(This article belongs to the Special Issue Catechin in Human Health and Disease)
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Abstract

Staphylococcal enterotoxin A (SEA) is a toxin protein, and is the most common cause of staphylococcal food poisoning. Polyphenols, such as catechins, are known to interact with proteins. In this study, we investigated the binding of catechins to SEA using SPR (Biacore), Fourier transform infrared spectroscopy (FT-IR), isothermal titration calorimetry (ITC), and protein-ligand docking. We found that (−)-epigallocatechin gallate (EGCG) could strongly bind to SEA. According to thermodynamic parameters, a negative ΔG indicated that the interaction between EGCG and SEA was spontaneous, and the electrostatic force accompanied by hydrophobic binding forces may play a major role in the binding. Data from Western blot analysis and docking simulation suggest that the hydroxyl group at position 3 of the galloyl group in the catechin structure was responsible for binding affinity with the Y91 of the A-6 region of SEA active sites. Our results provide further understanding of the binding interactions between catechins and SEA, and the inhibition of toxin activities by catechins. View Full-Text
Keywords: staphylococcal enterotoxin A; catechins; (−)-epigallocatechin gallate; molecular docking staphylococcal enterotoxin A; catechins; (−)-epigallocatechin gallate; molecular docking
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Shimamura, Y.; Utsumi, M.; Hirai, C.; Nakano, S.; Ito, S.; Tsuji, A.; Ishii, T.; Hosoya, T.; Kan, T.; Ohashi, N.; Masuda, S. Binding of Catechins to Staphylococcal Enterotoxin A. Molecules 2018, 23, 1125.

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