期刊
PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY
卷 50, 期 7, 页码 673-681出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/10826068.2020.1725774
关键词
Circular dichroism; fluorescence; lysozyme; protein aggregation; quinoline yellow
类别
资金
- Deanship of Scientific Research at King Saud University, Riyadh, Saudi Arabia
Quinoline yellow (QY) is a synthetic yellow dye widely used as a coloring agent for various foodstuffs. In the current study, we have examined the role of QY on the aggregation propensity of hen egg-white lysozyme (HEWL) under physiological conditions. The dye induced conformational changes in HEWL leading to aggregate formation were identified by circular dichroism (CD), turbidity analysis, fluorescence measurement and microscopic (TEM) imaging. Molecular docking and molecular dynamics simulation studies were also employed to strengthen binding and aggregation results. Our results indicate that 25-100 mu M of QY induces aggregation in HEWL, while lower QY concentrations (5 and 10 mu M) does not have any effect on the aggregation propensity of HEWL. The kinetics of HEWL aggregation demonstrate nucleation independent aggregation of HEWL without lag phase. On the other hand, far UV-CD analysis illustrated the loss of alpha-helical structure with the increasing concentration of QY. TEM results also support the formation of aggregate structures in HEWL when exposed to QY. Molecular docking and simulation studies revealed that the HEWL-QY complex is stable as compared to individual entities. In silico analysis also illustrated that QY-induced aggregation of HEWL proceeds through the formation of hydrogen bonds, electrostatic (Pi-Anion) and Pi-Sulfur interactions. The above-mentioned results highlight the possible detrimental effect by food additive dyes, particularly in protein misfolding.
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