白藜芦醇
化学
结合常数
猝灭(荧光)
对接(动物)
结合位点
立体化学
荧光光谱法
生物化学
荧光
量子力学
医学
物理
护理部
作者
Mohd Aamir Qureshi,Saleem Javed
标识
DOI:10.1038/s41598-022-06375-5
摘要
Resveratrol is a polyphenol belonging to the class stilbenes. The active and stable form of resveratrol is trans-resveratrol. This polyphenol is bestowed with numerous biological properties. Aflatoxin B1 is a hepato-carcinogen and mutagen that is produced by Aspergillus species. In this study, the interaction of trans-resveratrol with HSA followed by competitive dislodging of AFB1 from HSA by trans-resveratrol has been investigated using spectroscopic studies. The UV-absorption studies revealed ground state complex formation between HSA and trans-resveratrol. Trans-resveratrol binds strongly to HSA with the binding constant of ~ 107 M-1 to a single binding site (n = 1.58), at 298.15 K. The Stern-Volmer quenching constant was calculated as 7.83 × 104 M-1 at 298.15 K, suggesting strong fluorescence quenching ability of trans-resveratrol. Site markers displacement assay projected subdomain IIA as the binding site of trans-resveratrol to HSA. The molecular docking approach envisages the amino acid residues involved in the formation of the binding pocket. As confirmed from the site marker displacement assays, both trans-resveratrol and AFB1 binds to HSA in the same binding site, subdomain IIA. The study explores the ability of trans-resveratrol to displace AFB1 from the HSA-AFB1 complex, thereby affecting the toxicokinetic behavior of AFB1 associated with AFB1 exposure.
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