Presentation Information

[14a-K507-3]Structure Analysis of Amyloid β Oligomers Linked at Two Positions

〇Chikara Harada1, Atsuya Matsui1,2, Yumi Irie3, Ayumi Uchino3, Ayaka Chikugo3, Kotaro Fujii1, Katsuma Hosoi1, Akio Nakanishi1, Yusuke Kageyama1, Nobuyasu Naruse1, Chihiro Tsukano3, Kazuhiro Irie3,4, Yutaka Mera1 (1.Shiga Univ. of Med. Sci., 2.General Care & Education Tennri Hosp., 3.Kyoto Univ., 4.Doshisya Univ.)

Keywords:

amyloid β,atomic force microscopy

In pathological research on Alzheimer’s disease, amyloid β (Aβ) oligomers are considered to play a crucial role, but their diverse forms and types have made detailed analysis challenging. In this study, a method was established to precisely analyze height information using atomic force microscopy (AFM) by artificially synthesizing Aβ dimers and trimers to control their morphology. Aβ dimers were observed as spherical particles, and histogram analysis of their height distribution revealed peaks suggesting the presence of intermolecular parallel β-sheet structures.

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