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Inhibiting Aggregation of β‐Amyloid by Folded and Unfolded Forms of Fimbrial Protein of Gram‐Negative Bacteria.

Authors :
Yamamoto, Keisuke
Oyaizu, Misa
Takahashi, Tsuyoshi
Watanabe, Yoshihito
Shoji, Osami
Source :
ChemistrySelect; 9/29/2017, Vol. 2 Issue 28, p9058-9062, 5p
Publication Year :
2017

Abstract

Abstract: 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
23656549
Volume :
2
Issue :
28
Database :
Complementary Index
Journal :
ChemistrySelect
Publication Type :
Academic Journal
Accession number :
130770671
Full Text :
https://doi.org/10.1002/slct.201700658