Development of functional proteins based on self-assembly of denatured proteins

2015 Fiscal Year Final Research Report

• Project/Area Number: 15K13740
• Research Category: Grant-in-Aid for Challenging Exploratory Research
• Allocation Type: Multi-year Fund
• Research Field: Bio-related chemistry
• Research Institution: Nagoya University
• Principal Investigator: Shoji Osami 名古屋大学, 理学(系)研究科(研究院), 准教授 (90379587)
• Project Period (FY): 2015-04-01 – 2016-03-31
• Keywords: 変性蛋白質 / 自己集合 / 繊毛 / ベータシート構造 / アミロイド繊維 / アルツハイマー病

Outline of Final Research Achievements

The pilus part of Type I fimbria found on the surface of Gram-negative bacteria is composed of multiple copies of FimA and the last piece of FimA is linked to FimH via FimF and FimG. Each structural unit has an immunoglobulin (Ig)-like fold, which is formed from two-layered β-sheets. We have found that a soluble but denatured form of FimG protein can accommodate various hydrophobic molecules. Inhibiting the self-assembly of β-amyloid (Aβ) is considered to be one of the strategies through which to treat Alzheimer’s disease. Thus, we have tried to inhibit the self-assembly of Aβ using the denatured form of FimG and demonstrated that the denatured form of FimG prevents Aβ oligomerization.

Free Research Field

生体機能関連化学