2024-03-28T20:34:06Z
https://nagoya.repo.nii.ac.jp/oai
oai:nagoya.repo.nii.ac.jp:00025137
2023-01-16T04:14:22Z
336:695:696
Inhibiting Aggregation of β-Amyloid by Folded and Unfolded Forms of Fimbrial Protein of Gram-Negative Bacteria
Yamamoto, Keisuke
Oyaizu, Misa
Takahashi, Tsuyoshi
Watanabe, Yoshihito
Shoji, Osami
open access
This is the peer reviewed version of the following article: [K. Yamamoto, M. Oyaizu, T. Takahashi, Y. Watanabe, O. Shoji.(2017), Inhibiting Aggregation of β-Amyloid by Folded and Unfolded Forms of Fimbrial Protein of Gram-Negative Bacteria. ChemistrySelect,2:9058–9062. doi:10.1002/slct.201700658], which has been published in final form at [http://doi.org/10.1002/slct.201700658]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
Inhibition self-assembly of β-amyloid (Aβ) is considered to be a strategy that can be potentially useful to develop treatment for Alzheimer's disease (AD). We have discovered that a protein unit that is found in the fimbriae of Gram-negative bacteria, which has a vacant site for a β-sheet strand, prevents Aβ oligomerization effectively. Moreover, we found that a soluble but denatured form of this protein shows even higher potency. Our results also demonstrate the applicability of denatured proteins as pharmaceutical material.
Wiley
2017-09-29
eng
journal article
AM
http://hdl.handle.net/2237/27357
https://nagoya.repo.nii.ac.jp/records/25137
https://doi.org/10.1002/slct.201700658
2365-6549
ChemistrySelect
2
9058
9062
https://nagoya.repo.nii.ac.jp/record/25137/files/manuscript_slct_201700658R2.pdf
application/pdf
1.6 MB
2018-09-29