Sizes of amyloid-β oligomers predicted using atomic force microscopy and two-point crosslinked dimers as standards
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.
Authors
- Nobuyasu Naruse (ORCID: https://orcid.org/0000-0003-3934-2641)
- Chihiro Tsukano (ORCID: https://orcid.org/0000-0002-9361-0857)
- A. Nakanishi (ORCID: https://orcid.org/0000-0002-6572-0055)
- Kotaro Fujii (ORCID: https://orcid.org/0000-0003-3309-9118)
- Kazuhiro Irie (ORCID: https://orcid.org/0000-0001-7109-8568)
- Ayumi Uchino (ORCID: https://orcid.org/0000-0003-4793-6618)
- Yumi Irie
- Yusuke Kageyama (ORCID: https://orcid.org/0000-0002-3382-9881)
- Yutaka Mera (ORCID: https://orcid.org/0000-0003-4090-3530)
- Atsuya Matsui
- Chihiro Harada
- Katsuma Hosoi
- Ayaka Chikugo
Institutions
- Doshisha University (JP)
- Shiga University of Medical Science (JP)
- Kyoto University (JP)
- Tenri Hospital (JP)
Publication Details
- Journal
- Chemical Communications
- Published
- 2025-01-01
- DOI
- https://doi.org/10.1039/d5cc00856e
- Primary Topic
- Alzheimer's disease research and treatments
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Japan Society for the Promotion of Science