期刊
ACS OMEGA
卷 6, 期 33, 页码 21579-21585出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsomega.1c02593
关键词
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资金
- Inner Mongolia Autonomous Region Applied Technology Research and Development Fund Project [2019GG240]
- Distinguished Young Scholars Foundation of Inner Mongolia Autonomous Region [2018JQO4]
- Young Leading Talents of Science and Technology Program of Inner Mongolia Autonomous Region [NJYT-18-A04]
- National Natural Science Foundation of China [51763019, U1832125]
The study demonstrates that isorhamnetin, kaempferol, myricetin, and quercetin in sea buckthorn can interact with tyrosinase, inhibiting its catalytic activity. Among these compounds, quercetin shows the lowest binding energy and the most stable complex with tyrosinase, potentially serving as a natural inhibitor for tyrosinase.
Isorhamnetin, kaempferol, myricetin, and quercetin are four kinds of secondary metabolites in sea buckthorn, which have a wide range of biological activities. Investigating their interactions with tyrosinase at the atomic level can improve the bioavailability of sea buckthorn. Both molecular docking and molecular dynamics simulation methods were employed to study the interactions of these ligands with tyrosinase. The results of molecular docking indicated that these four small molecules such as isorhamnetin, kaempferol, myricetin, and quercetin can all dock into the active center of tyrosinase, and by occupying the active site, they can prevent substrate binding, thereby reducing the catalytic activity of tyrosinase. Molecular dynamics simulation trajectory analysis showed that all tyrosinase-ligand complexes reach an equilibrium within 100 ns. In addition, quercetin has the lowest binding energy among these four ligands, and the complex with tyrosinase is the most stable. This study not only provides valuable information for improving the bioavailability of sea buckthorn but also contributes to the discovery of effective natural inhibitors of tyrosinase.
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