Binding of Catechins to Staphylococcal Enterotoxin A

被引：19

作者：

Shimamura, Yuko ^{[1
]}

Utsumi, Mio ^{[1
]}

Hirai, Chikako ^{[1
]}

Nakano, Shogo ^{[1
]}

Ito, Sohei ^{[1
]}

Tsuji, Ai ^{[2
,5
]}

Ishii, Takeshi ^{[2
]}

Hosoya, Takahiro ^{[3
,6
]}

Kan, Toshiyuki ^{[4
]}

Ohashi, Norio ^{[1
]}

Masuda, Shuichi ^{[1
]}

机构：

[1] Univ Shizuoka, Sch Food & Nutr Sci, Suruga Ku, 52-1 Yada, Shizuoka 4228526, Japan

[2] Kobe Gakuin Univ, Fac Nutr, Nishi Ku, 518 Arise,Ikawadani Cho, Kobe, Hyogo 6512180, Japan

[3] Yokohama Univ Pharm, Dept Kampo Pharm, Totsuka Ku, 601 Matano Cho, Yokohama, Kanagawa 2450066, Japan

[4] Univ Shizuoka, Sch Pharmaceut Sci, Dept Synthet Organ & Med Chem, Suruga Ku, 52-1 Yada, Shizuoka 4228526, Japan

[5] Nara Womens Univ, Dept Food Sci & Nutr, Kita Uoya Nishimachi, Nara 6308506, Japan

[6] Toyo Univ, Dept Nutr & Hlth Sci, Fac Food & Nutr Sci, 1-1-1 Izumino, Itakura, Gunma 3740193, Japan

来源：

MOLECULES | 2018年 / 23卷 / 05期

关键词：

staphylococcal enterotoxin A; catechins; (-)-epigallocatechin gallate; molecular docking; ISOTHERMAL TITRATION CALORIMETRY; GREEN TEA POLYPHENOL; HUMAN SERUM-ALBUMIN; LIPID-BILAYERS; EPIGALLOCATECHIN GALLATE; AUREUS ENTEROTOXINS; (-)-EPIGALLOCATECHIN-3-GALLATE; FLUORESCENCE; RECOGNITION; INHIBITION;

D O I：

10.3390/molecules23051125

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 G 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.

引用

页数：13