Forming nanoconjugates or inducing macroaggregates, curcumin dose effect on myosin assembling revealed by molecular dynamics simulation
Forming nanoconjugates or inducing macroaggregates, curcumin dose effect on myosin assembling revealed by molecular dynamics simulation
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DOI：
10.1016/j.colsurfa.2020.125415
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发表时间：
2020-12
期刊：
影响因子：
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通讯作者：
Li Zhang;Jian Sun;Yue Qi;Yaqi Song;Zongyun Yang;Zhen Li;Lei Liu;Peng Wang;Xinglian Xu;G. Zhou
中科院分区：
文献类型：
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作者：
Li Zhang;Jian Sun;Yue Qi;Yaqi Song;Zongyun Yang;Zhen Li;Lei Liu;Peng Wang;Xinglian Xu;G. Zhou
本工作通过一种简单有效的方法将姜黄素包埋到肌球蛋白中。与游离姜黄素相比，微囊化的姜黄素具有更好的抗氧化性、储存稳定性和热稳定性，具有潜在的工业应用前景。在固定的蛋白质浓度下，低浓度姜黄素(40−80μg/mL)的肌球蛋白-姜黄素分散体具有很强的稳定性，纳米粒的包封率在80%以上，而姜黄素浓度过高则会形成较大的肌球蛋白聚集体。分子动力学模拟表明，姜黄素的自缔合作用是蛋白质聚集的主要原因。姜黄素形成分子堆栈，连接两侧的蛋白质链，诱导蛋白质接近。肌球蛋白颗粒相互缠绕，形成大的聚集体。这项工作证明了肌球蛋白可以作为姜黄素的全天然递送系统，为姜黄素和蛋白质在食品和生物医学应用中的未来组装提供了指导。
The present work we have encapsulated curcumin into myosin by a simple and effective strategy. Compared with free curcumin, the encapsulated curcumin possessed improved antioxidant activity, storage stability, and thermal stability and thus exhibited potential for industrial applications. At fixed protein concentration, myosin-curcumin dispersion at low concentration of curcumin (40−80 μg/mL) exhibited strong stability with the encapsulation efficiencies of the nanoparticles above 80 %, whereas excessive curcumin concentration led to the formation of large myosin aggregates. Molecular dynamics simulation suggested that curcumin self-association was the main reason for protein aggregation. Curcumin formed molecular stacks, which bridged the protein chains on both sides and induced protein proximity. Myosin particles entangled with one another to form large aggregates. This work demonstrated that myosin can be an all-natural delivery system for curcumin and provided guidance for the future assembly of curcumin and protein in food and biomedical applications.