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

抄録

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.

収録刊行物

• ChemistrySelect

  ChemistrySelect 2 9058-9062, 2017-09-29

  Wiley

キーワード

• General Chemistry

詳細情報

• CRID: 1050001338805943552
• NII論文ID: 120006382268
• DOI: 10.1002/slct.201700658
• ISSN: 23656549
• HANDLE: 2237/27357
• Web Site: https://nagoya.repo.nii.ac.jp/records/25137
• Web Site: https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fslct.201700658
• Web Site: https://onlinelibrary.wiley.com/doi/full/10.1002/slct.201700658
• 本文言語コード: en
• 資料種別: journal article
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