Aflatoxin B1 Induced Structural and Conformational Changes in Bovine Serum Albumin: A Multispectroscopic and Circular Dichroism-Based Study

Aflatoxin B-1 (AFB(1)) is a mutagen that has been categorized as a group 1 human carcinogen by the International Agency for Research on Cancer. It is produced as a secondary metabolite by soil fungi Aspergillus flavus and Aspergillus parasiticus. Here, in this study, the effect of AFB(1) on the structure and conformation of bovine serum albumin (BSA) using multispectroscopic tools like fluorescence spectroscopy, ultraviolet-visible absorption spectroscopy, and circular dichroism spectropolarimetry has been ascertained. Ultraviolet absorption spectroscopy revealed hyperchromicity in the absorption spectra of BSA in the presence of AFB(1). The binding constant was calculated in the range of 10(4) M-1, by fluorescence spectroscopy suggesting moderate binding of the toxin to BSA. The study also confirms the static nature of fluorescence quenching. The stoichiometry of binding sites was found to be unity. The competing capability of warfarin for AFB(1) was higher than ibuprofen as calculated from site marker displacement assay. Forster resonance energy transfer confirmed the high efficiency of energy transfer from BSA to AFB(1). Circular dichroism spectropolarimetry showed a decrease in the a-helix in BSA in the presence of AFB(1). The melting temperature of BSA underwent an increment in the presence of a mycotoxin from 62.5 to 70.3 degrees C. Molecular docking confirmed the binding of AFB(1) to subdomain IIA in BSA.

Automated summary

This study utilized multispectroscopic tools to investigate the effect of Aflatoxin B-1 on the structure and conformation of bovine serum albumin. The results showed moderate binding of the toxin to BSA, a decrease in the alpha helix structure, and an increase in the melting temperature of BSA in the presence of the mycotoxin. Molecular docking confirmed the binding of AFB(1) to subdomain IIA in BSA.