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Investigation on the interaction of food colorant Sudan III with bovine serum albumin using spectroscopic and molecular docking methods
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 × 102 L·mol−1 to 0.69 and 5.83 × 102 L·mol−1 at 298 and 310 K, respectively. The enthalpy change (ΔH) and entropy change (ΔS) 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.
Investigation on the interaction of food colorant Sudan III with bovine serum albumin using spectroscopic and molecular docking methods
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 × 102 L·mol−1 to 0.69 and 5.83 × 102 L·mol−1 at 298 and 310 K, respectively. The enthalpy change (ΔH) and entropy change (ΔS) 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.
Investigation on the interaction of food colorant Sudan III with bovine serum albumin using spectroscopic and molecular docking methods
Bai, Jie (author) / Ma, Xiping (author) / Sun, Xuekai (author)
Journal of Environmental Science and Health, Part A ; 55 ; 669-676
2020-05-11
8 pages
Article (Journal)
Electronic Resource
English
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