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- Title
Molecular Insight into the Binding of Astilbin with Human Serum Albumin and Its Effect on Antioxidant Characteristics of Astilbin.
- Authors
Han, Xiangyu; Sun, Jing; Niu, Tianmei; Mao, Beibei; Gao, Shijie; Zhao, Pan; Sun, Linlin
- Abstract
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.
- Subjects
SERUM albumin; HYDROGEN bonding interactions; MOLECULAR dynamics; OXIDANT status; FLUORESCENCE quenching; FERTILIZERS
- Publication
Molecules, 2022, Vol 27, Issue 14, pN.PAG
- ISSN
1420-3049
- Publication type
Article
- DOI
10.3390/molecules27144487