Studies on the interactions of theaflavin-3,3 '-digallate with bovine serum albumin: Multi-spectroscopic analysis and molecular docking
文献类型： 外文期刊
作者： Yu, Xia 1 ; Cai, Xinghong 2 ; Li, Shuang 3 ; Luo, Liyong 1 ; Wang, Jie 5 ; Wang, Min 2 ; Zeng, Liang 1 ;
作者机构： 1.Southwest Univ, Coll Food Sci, 2 Tiansheng Rd, Chongqing 400715, Peoples R China
2.Southwest Univ, Sch Mat & Energy, 2 Tiansheng Rd, Chongqing 400715, Peoples R China
3.Kaijiang Cty Bur Agr & Rural Affairs, Dazhou 635000, Kaijiang County, Peoples R China
4.Southwest Univ, Tea Res Inst, 2 Tiansheng Rd, Chongqing 400715, Peoples R China
5.Chongqing Acad Agr Sci, Tea Res Inst, Chongqing 402160, Peoples R China
关键词： Theaflavin-3, 3 '-digallate; Interaction; Fourier-transform infrared spectroscopy; Molecular docking
期刊名称：FOOD CHEMISTRY （ 影响因子：8.5； 五年影响因子：8.2 ）
ISSN： 0308-8146
年卷期： 2022 年 366 卷
页码：
收录情况： SCI
摘要： Tea cream, produced by interactions among tea ingredients, is undesirable in tea beverage industry. The interaction between bovine serum albumin (BSA) and theaflavin-3,3'-digallate (TFDG, an important component in tea cream and functional substance of black tea) was investigated by fluorescence spectroscopy, ultraviolet-visible (UV-vis) absorption spectroscopy, synchronous fluorescence spectroscopy, fourier-transform infrared (FT-IR) spectroscopy, and molecular docking technique. Multi-spectroscopic experiments demonstrated that TFDG interacted with BSA via static quenching, and the microenvironment around BSA became more hydrophobicity. FT-IR showed that the alpha-helix of BSA was increased when binding with TFDG. Thermodynamic parameters and molecular docking demonstrated that hydrophobic interactions and hydrogen bonds dominated the interaction between TFDG and BSA. The mechanism proposed in this research could further develop some nanoparticles to excellent biochemical properties while reducing the formation of tea cream, and explore the potential of BSA as transport carrier for TFDG
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