[1P01-32] Poster session

[1P30] Two-dimensional diffusivity and fibril formation of amyloid β protein on lipid membranes: a comparison of closed and open systems

*Sota Nishino¹, Toshinori Shimanouchi¹, Yukitaka Kimura¹ (1. Graduate School of Environmental, Life, Natural Science and Technology, Okayama University (Japan))

Amyloid β (Aβ) with a molecular weight of 4.3 kDa forms amyloid fibrils as key compounds in the pathological process of Alzheimer's disease (AD). A ganglioside, GM1, one of glycolipids, has been suggested to form “amyloid assemblages” that is an Aβ aggregate with no activity as an amyloid nucleus but catalytic activity for fibrillation. In this study, we examined the possibility of amyloid assemblage formation. We prepared DOPC/GM1 giant vesicles with an internal aqueous phase space, as a “closed system” and a DOPC/GM1 planar lipid bilayer as an “open system”. Diffusion behavior of fluorescence-labelled Aβ with 1-40 amino acid sequence (FL-Aβ) were monitored in a manner of single molecular tracking. Diffusion of almost FL-Aβ were restricted. Diffusion length of FL-Aβ on closed system indicated was longer than that on open system. However, a similar diffusivity between closed and open systems was confirmed. Furthermore, it was found that initially aggregated Aβ did not grow into amyloid, neighboring Aβ grown up to fibril, suggesting that aggregated Aβ on the glycolipid-rich phase behaved as amyloid assemblage.

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