蛋白质凝集速率的定量和胰岛淀粉样多肽-抑制剂复合物的猝灭作用<a href="#fn1" title="提供电子补充信息（ESI）。参见DOI：10.1039 / c9cp03238j">†</a>,Physical Chemistry Chemical Physics

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蛋白质凝集速率的定量和胰岛淀粉样多肽-抑制剂复合物的猝灭作用 †
Physical Chemistry Chemical Physics ( IF 2.9 ) Pub Date : 2019-08-19 00:00:00 , DOI: 10.1039/c9cp03238j
Suparna Khatun _{1,

2,

3,

4} , Anurag Singh _{1,

2,

3,

4} , Debabrata Mandal _{2,

3,

4,

5} , Amreesh Chandra _{1,

2,

3,

4,

5} , Amar Nath Gupta _{1,

2,

3,

4}

Affiliation

淀粉样蛋白聚集体的形成是许多蛋白质错误折叠疾病（包括II型糖尿病）的标志，该疾病是由淀粉样蛋白的原纤维化引起的。已经确定，诸如姜黄素，白藜芦醇和石墨烯量子点的纳米级配体可以改变蛋白质聚集速率。在本文中，我们报告了对这些配体的比较研究，以使用各种实验技术估算它们的蛋白质聚集速率和荧光猝灭。通过光散射实验，R _H发现裸露的胰岛淀粉样多肽以每天43％的速度增加，而在不同摩尔比的配体（A1C10，A1R10和A1GQDs20）存在下，发现配合物的大小以7％的速度增长，每天分别为8％和13％。我们使用光致发光实验观察了所有三种蛋白质-配体复合物的荧光猝灭。蛋白质的聚集速率和荧光猝灭在抑制过程中表现出浓度依赖性的竞争作用。有趣的是，对于石墨烯量子点，蛋白质聚集率在较低浓度下受到更大的影响，而荧光猝灭在较高浓度下占主导。这与姜黄素和白藜芦醇相反，姜黄素和白藜芦醇在复合物中配体的所有浓度下荧光猝灭均占主导。FTIR数据显示，对于所有三种胰岛淀粉样多肽-配体比率，β-折叠明显转化为较少聚集倾向的二级结构。然而，姜黄素的抑制作用盖过了其他两种抑制剂的抑制作用。通过分析原纤维的分析和高分辨率TEM图像，证实了这三种配体的抑制行为。

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Quantification of protein aggregation rates and quenching effects of amylin–inhibitor complexes†

The formation of amyloid aggregates is the hallmark of many protein misfolding diseases, including Type-II diabetes mellitus, which is caused by the fibrillation of amylin protein. It is established that nano-sized ligands such as curcumin, resveratrol and graphene quantum dots can modify protein aggregation rates. In this article, we report a comparative study of these ligands to estimate their protein aggregation rates and fluorescence quenching using various experimental techniques. Through light scattering experiments, the R_H of bare amylin was found to increase at a rate of 43% per day, whereas in the presence of the ligands in different molar ratios (A1C10, A1R10 and A1GQDs20), the sizes of the complexes were found to grow at rates of 7%, 8% and 13% per day, respectively. We observed fluorescence quenching using photoluminescence experiments for all three protein–ligand complexes. The protein aggregation rate and fluorescence quenching exhibited a concentration-dependent competitive role in the inhibition process. Interestingly, for graphene quantum dots, the protein aggregation rate is more affected at lower concentrations, while fluorescence quenching dominates at higher concentrations; this is in contrast to curcumin and resveratrol, where fluorescence quenching dominates at all concentrations of the ligands in the complex. The FTIR data showed appreciable conversion of β-sheets into less aggregation-prone secondary structures for all three amylin–ligand ratios; however, the inhibition performance of curcumin overshadowed those of the other two inhibitors. The inhibition behavior of these three ligands was corroborated by analysis of analytical and high-resolution TEM images of the fibrils.

更新日期：2019-08-19

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