Sizes of amyloid-β oligomers predicted using atomic force microscopy and two-point crosslinked dimers as standards

Chikara Harada; Atsuya Matsui; Yumi Irie; Ayumi Uchino; Ayaka Chikugo; Kotaro Fujii; Katsuma Hosoi; Akio Nakanishi; Yusuke Kageyama; Nobuyasu Naruse; Chihiro Tsukano; Kazuhiro Irie; Yutaka Mera

doi:10.1039/D5CC00856E

Sizes of amyloid-β oligomers predicted using atomic force microscopy and two-point crosslinked dimers as standards†

Chikara Harada,‡^a Atsuya Matsui,‡^ab Yumi Irie,^c Ayumi Uchino,^c Ayaka Chikugo,^c Kotaro Fujii,^a Katsuma Hosoi,^d Akio Nakanishi,^a Yusuke Kageyama,^d Nobuyasu Naruse,

*^a Chihiro Tsukano,

^c Kazuhiro Irie

*^ce and Yutaka Mera

^a

Author affiliations

* Corresponding authors

^a Fundamental Bioscience (Physics), Shiga University of Medical Science, Shiga, Japan
E-mail: naruse@belle.shiga-med.ac.jp

^b General Care and Education, Tenri Hospital, Nara, Japan

^c Division of Food Science & Biotechnology, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan
E-mail: irie.kazuhiro.2z@kyoto-u.jp

^d Human Pathology, Shiga University of Medical Science, Shiga, Japan

^e Organization for Research Initiatives and Development, Doshisha University, Kyoto, Japan

Abstract

Herein, we investigate a two-point crosslinked amyloid-β (Aβ) dimer, which forms an intermolecular β-sheet. The atomic force microscopy statistical results indicate that the heights of these dimers are approximately 0.37 nm, providing a baseline for the Aβ peptide sizes and improving our understanding of Aβ oligomers in Alzheimer's disease.

Chemical Communications

Sizes of amyloid-β oligomers predicted using atomic force microscopy and two-point crosslinked dimers as standards†

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Sizes of amyloid-β oligomers predicted using atomic force microscopy and two-point crosslinked dimers as standards

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