期刊
FOOD HYDROCOLLOIDS
卷 101, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2019.105455
关键词
Curcumin; Myosin; Interaction; Molecular dynamics simulation
资金
- Fundamental Research Funds for the Central Universities [KYDS201812, KYZ201652]
- National Natural Science Foundation [31571769]
- China Agricultural Research System [CARS-41]
This study aimed to reveal the interaction of curcumin with myosin and explore the potential of this meat protein as delivery system for curcumin. The curcumin/myosin complex was confirmed by UV-Vis spectroscopy, and fluorescence spectra suggested a static quenching in the binding with strong affinity of 1.5 x 10(5) M-1. CD studies indicated that the interaction between curcumin and myosin caused slight changes in the secondary structure of the protein, which was consistent with the results of molecular dynamics observations. Furthermore, hydrophobic interaction and hydrogen bond were observed to promote the curcumin-myosin complexation by molecular dynamics simulation technique. Molecular simulation results suggested that curcumin tends to combined with the residues 801-850 in the head region of protein, 1156-1195, and 1739-1743 of A chain, 1162-1218, and 1736-1745 of B chain in the tail region over the course of curcumin and myosin interaction. The presented study contributes to extend the potential application of meat protein as delivery system for curcumin.
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