Probing the mechanism of interaction between capsaicin and myofibrillar proteins through multispectral, molecular docking, and molecular dynamics simulation methods
文献类型: 外文期刊
作者: Wu, Zhicheng 1 ; Xu, Jingbing 4 ; Ruan, Jinggang 1 ; Chen, Jiaxin 1 ; Li, Xue 5 ; Yu, Yiru 1 ; Xie, Xinrui 1 ; Tang, Jie 1 ; Zhang, Dong 1 ; Li, Hongjun 6 ;
作者机构: 1.Xihua Univ, Coll Food & Bioengn, Chengdu 610039, Peoples R China
2.Chongqing Key Lab Special Food Cobuilt Sichuan & C, Chengdu 610039, Peoples R China
3.Xihua Univ, Food Ind Collaborat Innovat Ctr, Chengdu 610039, Peoples R China
4.Chongqing Inst Food & Drug Control, Chongqing 401121, Peoples R China
5.Chongqing Acad Agr Sci, Agr Prod Proc Inst, Chongqing 401329, Peoples R China
6.Southwest Univ, Coll Food Sci, Chongqing 400715, Peoples R China
关键词: Capsaicin; Myofibrillar proteins; Interaction mechanisms; Multispectral; Molecular docking; Molecular dynamics simulation
期刊名称:FOOD CHEMISTRY-X ( 影响因子:6.1; 五年影响因子:6.4 )
ISSN: 2590-1575
年卷期: 2023 年 18 卷
页码:
收录情况: SCI
摘要: The interaction between myofibrillar proteins (MPs) and capsaicin (CAP) was investigated using multispectral, molecular docking, and molecular dynamics simulation methods. The resulting complex increased the hydrophobicity of the tryptophan and tyrosine microenvironment as revealed by fluorescence spectral analysis. The fluorescence burst mechanism study indicated that the fluorescence burst of CAP on the MPs was a static one (Kq = 1.386 x 1012 m-1s 1) and that CAP could bind with MPs well (Ka = 3.31 x 104 L/mol, n = 1.09). The analysis of circular dichroism demonstrated that the interaction between CAP and MPs caused a decrease in the & alpha;-helical structure of MPs. The complexes formed exhibited lower particle size and higher absolute & zeta; potential. Furthermore, hydrogen bonding, van der Waals forces, and hydrophobic interactions were found to be the primary factors facilitating the interaction between CAP and MPs, as suggested by molecular docking models and molecular dynamics simulations.
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