The 81st JSAP Autumn Meeting, 2020

Presentation information

Oral presentation

12 Organic Molecules and Bioelectronics » 12.6 Nanobiotechnology

[11a-Z12-1~10] 12.6 Nanobiotechnology

Fri. Sep 11, 2020 8:30 AM - 11:30 AM Z12

Koji Sumitomo(Univ. of Hyogo), Yoichiroh Hosokawa(NAIST), Takeo Miyake(Waseda Univ.)

8:30 AM - 8:45 AM

[11a-Z12-1] Observation of aggregation and fibrillization of α-Synuclein on liposomes immobilized on Au electrode surface by AFM in liquid

〇(M2)Ryoko Kobayashi1, Masanori Sawamura2, Hodaka Yamakado2, Noda Minoru1 (1.Kyoto Inst. Tech., 2.Kyoto Univ.)

Keywords: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. Accordingly, the detection of a trace amount of the αSyn fibril is essential for early diagnosis of PD.
We have previously applied the methods of protein misfolding cyclic amplification (PMCA) and real-time quaking-induced conversion (RT-QuIC) 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. The aggregation of αSyn on the liposome-immobilized cantilever surface has not been observed so far qualitatively and quantitatively. In this study, therefore, the chronological behavior and interaction of αSyn with liposomes immobilized on the surface of the cantilever was examined by AFM in liquid. As a recent result, an aggregate as large as about 50 nm was observed on the liposome after addition of αSyn.