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Molecular interaction of soybean protein and piperine by computational docking analyses

文献类型： 外文期刊

作者： Zhang, Chaohua 1 ; Niu, Zhiqiang 2 ; He, Zhiliang 2 ; Ding, Yunshuang 1 ; Wu, Guiping 1 ; Wu, Haifeng 6 ; Chen, Weijun 4 ; Dong, Conghui 5 ; Ye, Zan 5 ; Gu, Fenglin 1 ; Hu, Weicheng 2 ;

作者机构： 1.Chinese Acad Trop Agr Sci, Spice & Beverage Res Inst, Wanning 571533, Hainan, Peoples R China

2.Yangzhou Univ, Inst Translat Med, Sch Med, Yangzhou 225009, Peoples R China

3.Chinese Acad Trop Agr Sci, Sanya Res Inst, Sanya 572025, Hainan, Peoples R China

4.Hainan Univ, Coll Food Sci & Engn, Haikou 570228, Hainan, Peoples R China

5.Key Lab Proc Suitabil & Qual Control Special Trop, Wanning 571533, Hainan, Peoples R China

6.Chinese Acad Med Sci & Peking Union Med Coll, Inst Med Plant Dev, Beijing Key Lab New Drug Discovery Based Class Chi, Key Lab Bioact Subst & Resources Utilizat Chinese, Beijing 100193, Peoples R China

关键词： Piperine; Soybean protein; Structure; Molecular dynamics simulations; Docking study

期刊名称：FOOD HYDROCOLLOIDS （ 影响因子：10.7； 五年影响因子：10.9 ）

ISSN： 0268-005X

年卷期： 2024 年 146 卷

页码：

收录情况： SCI

摘要： This study investigated the interaction of soybean glycinin (11S) and beta-conglycinin (7S) proteins with piperine (PIP) and compared the differences between them. Molecular docking results showed that PIP bound to 11S and 7S mainly through electrostatic, hydrogen bonding, and hydrophobic interactions to form complexes with desirable microstructures, leading to a decrease in the surface hydrophobicity of 7S/11S protein. In particular, the decrease for 11S protein was more pronounced than that for 7S protein, and the affinity of PIP for 11S protein was higher than that for 7S protein. Molecular dynamics (MD) results showed that the binding of PIP to soybean protein was spontaneous. The addition of PIP could cause different changes in the secondary structure of 7S/11S protein, mainly a decrease in beta-sheet and an increase in unordered coil, leading to the unfolding of soybean protein. This study provides a theoretical reference and research basis for elucidating the interaction mechanism between PIP and soybean protein in food systems, which is conducive to the potential application of soybean protein -PIP binding system in the food field.

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