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

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.