Journal
MOLECULES
Volume 27, Issue 14, Pages -Publisher
MDPI
DOI: 10.3390/molecules27144487
Keywords
astilbin; human serum albumin; multi-spectroscopic; molecular docking; molecular dynamics simulation; anti-oxidation
Funding
- National Natural Science Foundation of China [81903780]
- Shandong Provincial Natural Science Foundation [ZR2019BB031]
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This study investigated the interaction between astilbin and human serum albumin (HSA) and their effects on the antioxidant activity of astilbin. The results showed that astilbin quenches the fluorescence emission of HSA through a static quenching mechanism and preferentially binds at the Site I position. The presence of HSA also reduced the antioxidant capacity of astilbin, indicating potential effects on its clinical use.
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.
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