@article{oai:nagoya.repo.nii.ac.jp:00025137, author = {Yamamoto, Keisuke and Oyaizu, Misa and Takahashi, Tsuyoshi and Watanabe, Yoshihito and Shoji, Osami}, journal = {ChemistrySelect}, month = {Sep}, note = {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.}, pages = {9058--9062}, title = {Inhibiting Aggregation of β-Amyloid by Folded and Unfolded Forms of Fimbrial Protein of Gram-Negative Bacteria}, volume = {2}, year = {2017} }