Citation: LI Song, LIU Fu-Feng, YU Lin-Ling, ZHAO Yan-Jiao, DONG Xiao-Yan. Dual Effect of Thioflavin T on the Nucleation Kinetics of Amyloid β-Protein 40[J]. Acta Physico-Chimica Sinica, ;2016, 32(6): 1391-1396. doi: 10.3866/PKU.WHXB201603221 shu

Dual Effect of Thioflavin T on the Nucleation Kinetics of Amyloid β-Protein 40

Key Laboratory of Systems Bioengineering of the Ministry of Education, Department of Biochemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, P. R. China

Received Date: 4 January 2016
Revised Date: 21 March 2016

Fund Project: The project was supported by the National Natural Science Foundation of China (21236005, 21376172, 21406160, 21576199).

The fluorescent dye thioflavin T (ThT) is widely used for the qualitative and quantitative detection of amyloid fibrils. However, many small-molecular inhibitors have been shown to compete with ThT in binding the fibrils and therefore greatly affect the ThT fluorescence. The effect of ThT on the aggregation kinetics of amyloid proteins is not yet fully understood. Here, using amyloid β-protein 40 (Aβ40) as a model system, we show that ThT significantly alters the aggregation kinetics of Aβ40 in a dose-dependent manner, leading to a decrease-increase trend in the lag time that represents the nucleation rate. Specifically, the lag time decreases as a function of ThT concentration at low ranges, but then begins to increase beyond a specific ThT concentration, which itself increases with Aβ40 concentration. By contrast, the elongation rate slowly increases with ThT concentration. As for the secondary structure and morphology of the fibrils, no significant effects of ThT are observed. Isothermal titration calorimetry suggests that the hydrophobic interaction dominates the binding of ThT to Aβ40. Based on these findings, a working mechanism of the dual effects of ThT on Aβ fibrillization is proposed. These results should aid our understanding of the molecular mechanism of ThT binding with Aβ and allow practical improvements in the measurement of the nucleation kinetics of Aβ fibrillization.
- Amyloid β-protein,
- Thioflavin T,
- Fluorescence kinetic assay,
- Nucleation,
- Molecular interaction
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