Investigating binding dynamics of trans resveratrol to HSA for an efficient displacement of aflatoxin B1 using spectroscopy and molecular simulation

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 B-1 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 AFB(1) 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 similar to 10(7) M-1 to a single binding site (n = 1.58), at 298.15 K. The Stern-Volmer quenching constant was calculated as 7.83 x 10(4) 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 AFB(1) binds to HSA in the same binding site, subdomain IIA. The study explores the ability of trans-resveratrol to displace AFB(1) from the HSA-AFB(1) complex, thereby affecting the toxicokinetic behavior of AFB(1) associated with AFB(1) exposure.

Automated summary

In this study, the interaction between trans-resveratrol and HSA, as well as its effect on AFB(1), was investigated using spectroscopic studies. The results showed the formation of a ground state complex between trans-resveratrol and HSA, with strong binding to a single site. Site marker displacement assays confirmed subdomain IIA as the binding site for trans-resveratrol. The study also explored the ability of trans-resveratrol to displace AFB(1) from the HSA-AFB(1) complex.