硫黄素T对淀粉样β-蛋白质40聚集成核动力学的双重影响（英文）
发布时间：2018-10-31 12:07
【摘要】：荧光染料硫黄素T常用于淀粉样纤维聚集过程的定性定量检测。虽然有研究表明,某些抑制淀粉样蛋白质聚集的小分子抑制剂会与硫黄素T相互作用,影响其测试结果。但硫黄素T如何影响淀粉样蛋白质的聚集成核动力学尚不清晰。本文以淀粉样β-蛋白质40(Aβ40)为模型,系统研究了硫黄素T对Aβ40聚集成核的影响。研究发现:硫黄素T能够显著改变Aβ40的聚集成核动力学,且影响程度与硫黄素T的浓度密切相关。即在低浓度硫黄素T存在下,Aβ40成核速率的延迟时间先随着硫黄素T浓度的升高而缩短,后随着硫黄素T浓度的升高延迟时间反而延长。但延伸的速率却随硫黄素T浓度的升高而缓慢增大。另外,硫黄素T基本不会影响Aβ40的二级结构和纤维形态。同时,等温滴定微量热实验结果表明,硫黄素T结合Aβ40之间的主要作用力为疏水相互作用。据此,本研究提出硫黄素T对Aβ40聚集成核动力学的双重影响机理。这些结果有助于进一步了解硫黄素T与淀粉样蛋白质的作用特点,为今后硫黄素T在Aβ40聚集成核动力学实验中的使用提供参考。
[Abstract]:Fluorescence dye thioflavone T is often used for qualitative and quantitative determination of amyloid fiber aggregation process. Although studies have shown that some small molecular inhibitors that inhibit the aggregation of amyloid proteins interact with thiocyanin T to influence their test results. However, it is not clear how sulfur T affects the aggregation of amyloid proteins into nuclear power. Using amyloid 尾 -protein 40 (A 尾 40) as a model, the effects of thiocyanin T on the aggregation and nucleation of A 尾 40 were studied systematically. It was found that thiocyanin T could significantly change the aggregation of A 尾 40 into nuclear power science, and the degree of influence was closely related to the concentration of thiocyanin T. In the presence of low concentration of thiocyanin T, the delay time of A 尾 40 nucleation rate was first shortened with the increase of S T concentration, and then prolonged with the increase of S T concentration. However, the rate of extension increased slowly with the increase of sulfur T concentration. In addition, thiocyanin T had little effect on the secondary structure and fiber morphology of A 尾 40. At the same time, the results of isothermal titration showed that hydrophobic interaction was the main force between thiocyanin T and A 尾 40. Based on this, the mechanism of the double effect of sulfur T on the aggregation of A 尾 40 into nuclear power is proposed. These results are helpful to further understand the interaction between thiocyanin T and amyloid protein, and provide a reference for the application of thiocyanin T in A 尾 40 aggregation nuclear power experiment in the future.
【作者单位】： 天津大学化工学院生物工程系系统生物工程教育部重点实验室;
【基金】：supported by the National Natural Science Foundation of China(21236005,21376172,21406160,21576199)~~
【分类号】：O641.3
，
本文编号：2302125
[Abstract]:Fluorescence dye thioflavone T is often used for qualitative and quantitative determination of amyloid fiber aggregation process. Although studies have shown that some small molecular inhibitors that inhibit the aggregation of amyloid proteins interact with thiocyanin T to influence their test results. However, it is not clear how sulfur T affects the aggregation of amyloid proteins into nuclear power. Using amyloid 尾 -protein 40 (A 尾 40) as a model, the effects of thiocyanin T on the aggregation and nucleation of A 尾 40 were studied systematically. It was found that thiocyanin T could significantly change the aggregation of A 尾 40 into nuclear power science, and the degree of influence was closely related to the concentration of thiocyanin T. In the presence of low concentration of thiocyanin T, the delay time of A 尾 40 nucleation rate was first shortened with the increase of S T concentration, and then prolonged with the increase of S T concentration. However, the rate of extension increased slowly with the increase of sulfur T concentration. In addition, thiocyanin T had little effect on the secondary structure and fiber morphology of A 尾 40. At the same time, the results of isothermal titration showed that hydrophobic interaction was the main force between thiocyanin T and A 尾 40. Based on this, the mechanism of the double effect of sulfur T on the aggregation of A 尾 40 into nuclear power is proposed. These results are helpful to further understand the interaction between thiocyanin T and amyloid protein, and provide a reference for the application of thiocyanin T in A 尾 40 aggregation nuclear power experiment in the future.
【作者单位】： 天津大学化工学院生物工程系系统生物工程教育部重点实验室;
【基金】：supported by the National Natural Science Foundation of China(21236005,21376172,21406160,21576199)~~
【分类号】：O641.3
，
本文编号：2302125
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