Molecular Insight into the Binding of Astilbin with Human Serum Albumin and Its Effect on Antioxidant Characteristics of Astilbin

被引:11
作者
Han, Xiangyu [1 ]
Sun, Jing [1 ,2 ]
Niu, Tianmei [1 ]
Mao, Beibei [1 ]
Gao, Shijie [3 ]
Zhao, Pan [1 ]
Sun, Linlin [1 ,3 ]
机构
[1] Shandong Univ Tradit Chinese Med, Coll Pharm, Jinan 250355, Peoples R China
[2] Beijing Univ Chinese Med, Sch Chinese Mat Med, Beijing 100029, Peoples R China
[3] Shandong Univ Tradit Chinese Med, Expt Ctr, Jinan 250355, Peoples R China
基金
中国国家自然科学基金;
关键词
astilbin; human serum albumin; multi-spectroscopic; molecular docking; molecular dynamics simulation; anti-oxidation; DYNAMIC SIMULATION; DOCKING; DRUG;
D O I
10.3390/molecules27144487
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Astilbin is a dihydroflavonol glycoside identified in many natural plants and functional food with promising biological activities which is used as an antioxidant in the pharmaceutical and food fields. This work investigated the interaction between astilbin and human serum albumin (HSA) and their effects on the antioxidant activity of astilbin by multi-spectroscopic and molecular modeling studies. The experimental results show that astilbin quenches the fluorescence emission of HSA through a static quenching mechanism. Astilbin and HSA prefer to bind at the Site I position, which is mainly maintained by electrostatic force, hydrophobic and hydrogen bonding interactions. Multi-spectroscopic and MD results indicate that the secondary structure of HSA could be changed because of the interaction of astilbin with HSA. DPPH radical scavenging assay shows that the presence of HSA reduces the antioxidant capacity of astilbin. The explication of astilbin-HSA binding mechanism will provide insights into clinical use and resource development of astilbin in food and pharmaceutical industries.
引用
收藏
页数:19
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