目的:研究儿茶酚异喹啉类物质1-甲基-6,7-二羟基-1,2,3,4-四氢异喹啉(salsolinol,Sal)对帕金森病关键蛋白α突触核蛋白(α-syulcein,α-syn)纤维化程度的影响。方法:将重组人源α-Syn蛋白与不同浓度的Sal共同孵育,通过ThT染色对α-Syn成纤维状况进行监测。同时,利用扫描电镜和激光共聚焦显微镜观察α-Syn与Sal共孵育后的形态变化。结果/结论:实验结果表明Sal具有将α-Syn稳定在寡聚体或者原纤维状态的能力,且呈浓度依赖性,Sal浓度越大,α-Syn纤维化进程越缓慢。这一发现为进一步研究α-Syn和儿茶酚异喹啉类物质在PD发生和发展过程中起到的作用提供了一定的实验依据。
Object This study was to explore the relationship between salsolinal(Sal) and the fi bration of α-synuclein(α-Syn). Method Recombinant humana α-Syn was incubated with different concentration of Sal, respectively. The fi bration of α-syn was investigated via thionfl avin T(thT) assay, confocal laser scanning microscopy and transmission electron microscopy(TEM). Results/Conclusion Consequently, it was found that Sal could able to stabilize α-Syn in the oligomer form or protofi brils, which was more toxic than the fi ber form. This result provides new evidence for understanding the pathogenesis of PD.