Demonstration of the abnormal conformational transition of amyloid proteins and it's application as an early diagnostic tool

在朊病毒疾病中，致病蛋白质的异常结构被传递给具有正常结构的蛋白质。在这项研究中，我们的目的是阐明是否异常结构的致病蛋白的多聚谷氨酰胺（polyQ）神经退行性疾病也可以传播，以及这种现象是否可以用于检测微量的异常polyQ蛋白。我们发现，向正常polyQ蛋白中添加微量的异常polyQ蛋白会导致蛋白质结构转变的加速。此外，为了检测具有异常结构的蛋白质，我们分析了涉及浊度和荧光的系统，发现它们都具有相同的灵敏度。我们还确定了polyQ蛋白的纯化方法，该方法可以高效地实现蛋白质的结构转变。

In the prion diseases, the abnormal structure of the disease-causing protein is transmitted to proteins with a normal structure. In this study, we aimed to elucidate whether the abnormal structure of the disease-causing proteins of the polyglutamine (polyQ) neurodegenerative diseases can also be transmitted, and whether this phenomenon could be used for detection of minute levels of abnormal polyQ proteins. We found that addition of a minute level of abnormal polyQ protein to normal polyQ proteins causes acceleration of the structural transition of the proteins. Furthermore, for detection of proteins with an abnormal structure, we analyzed systems involving both turbidity as well as fluorescence, and found that they both had equal sensitivity. We also determined a purification method of the polyQ protein that allows structural transition of the protein at high efficiency.