Sudan III is a coloring agent used in chemical industries and food additives. This article uses spectroscopic and molecular docking methods to investigate the interaction of Sudan III with bovine serum albumin (BSA) under a physiological condition. Spectroscopic analysis of the emission quenching revealed that the quenching mechanism of BSA by Sudan III was static. The binding sites and constants of Sudan III-BSA complex were observed to be from 0.72 and 6.41 x 10(2) L center dot mol(-1) to 0.69 and 5.83 x 10(2) L center dot mol(-1) at 298 and 310 K, respectively. The enthalpy change (Delta H) and entropy change (Delta S) revealed that van der Waals forces and hydrogen bonds stabilized the Sudan III-BSA complex. Energy transfer from tryptophan to Sudan III occurred by a fluorescence resonance energy transfer mechanism, and the r distance (3.32 nm) had been determined. The results of UV-Vis absorption, synchronous, three-dimensional fluorescence, and circular dichroism spectra showed that Sudan III induced conformational changes of BSA. Molecular docking studies revealed that Sudan III situated within subdomain IIA of BSA. A study on the interaction between Sudan III and BSA was of fundamental importance for providing more information about the potential toxicological effect of chemicals at the molecular level.
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