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

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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.