Elucidation of binding mechanism of dibutyl phthalate on bovine serum albumin by spectroscopic analysis and molecular docking method

Abstract

Dibutyl phthalate has been illegally used in beverages and directly affects the human health. Herein, the interaction occurred between dibutyl phthalate and bovine serum albumin was studied. The experimental results demonstrated that dibutyl phthalate could bind to bovine serum albumin and statically quench the intrinsic fluorescence of this protein. Circular dichroism measurements proved that the binding of dibutyl phthalate would lead to an obvious decrease of α-helix content in the bovine serum albumin. Molecular docking analysis clarified the fluorescence quenching mechanism, size distribution and zeta potential variation, conformational change of BSA, the site marker competitive fluorescence quenching and the interaction mechanism of dibutyl phthalate to bovine serum albumin. This work provided a useful information for the binding of dibutyl phthalate to protein.

Keywords: Bovine serum albumin; Circular dichroism; Dibutyl phthalate; Fluorescence; Molecular docking; UV absorption spectra.