10:00 AM - 10:15 AM
△ [12a-A408-5] Detection of fibrillization of human-derived α-Synuclein by liposome-immobilized cantilever microsensor
Keywords:biosensor, alpha-synclein, liposome
α-synuclein (αSyn) has been majorly recognized as causative agent for Parkinson Disease (PD). Its monomer usually existing in our brain cell starts to aggregate and grow as oligomers, protofibrils and fibrils, which are recognized to be toxic. Therefore, the detection of the αSyn fibril is essential for early diagnosis of PD.
We have previously applied real-time quaking-induced conversion (RT-QuIC) method for label-free liposome-immobilized cantilever sensor in order to obtain a trace amount of chronological behavior of mouse-derived αSyn, realizing its fibrillar detection as small as 700 fM, which showed nearly the same detectivity as recent ELISA’s. This time, we proceeded to detect human-derived αSyn fibrillization with the same low concentration, although the fibrillization of human-derived is recognized less active than that of mouse-derived. Finally, we successfully detected the fibrillization of the human-derived with the same low concentration as the mouse-derived.
We have previously applied real-time quaking-induced conversion (RT-QuIC) method for label-free liposome-immobilized cantilever sensor in order to obtain a trace amount of chronological behavior of mouse-derived αSyn, realizing its fibrillar detection as small as 700 fM, which showed nearly the same detectivity as recent ELISA’s. This time, we proceeded to detect human-derived αSyn fibrillization with the same low concentration, although the fibrillization of human-derived is recognized less active than that of mouse-derived. Finally, we successfully detected the fibrillization of the human-derived with the same low concentration as the mouse-derived.