Exploring the mode of binding between butylated hydroxyanisole with bovine serum albumin: Multispectroscopic and molecular docking study

Considering the harm of BHA on humans, thorough research of the effect of BHA on the structure of serum albumin is necessary. The binding mechanisms of BHA with bovine serum albumin (BSA) and the effects of other three food additives (butylated hydroxytoluene, benzoic acid and citric acid) on BHA-BSA system were researched by multispectroscopy and molecular docking. The fluorescence quenching experiment results showed that the fluorescence quenching mechanism of BSA by BHA was static quenching. The binding constant ((5.70 +/- 0.38) x 103 M-1 at 298 K) and thermodynamic parameters (All = 110.8 +/- 2.91 kJ center dot mol-1 and AS = 443.3 +/- 9.30 J center dot mol-1 center dot K-1) indicated that BHA and BSA formed a relatively stable complex through hydrophobic interaction. Three-dimensional fluorescence spectra confirmed the conformation changes of BSA due to the binding of BHA. Site marker competitive experiments and molecular docking proved that BHA could bind BSA into site I in subdomain IIA. The results of molecular docking showed that BHA formed hydrophobic interactions with amino acid residues (Ala290, Leu237, Leu259, Ile263 and Ile289). The presence of other food additives weakened the binding of BHA to BSA.

Automated summary

The study found that the binding of BHA to serum albumin occurs through static quenching, forming a relatively stable complex with hydrophobic interactions as the main binding mechanism. BHA has the capability to bind to specific sites on BSA, and the presence of other food additives weakens the binding of BHA to BSA.