Structural basis of the self-propagation of amyloid fibrils and its manifestation

2015 Fiscal Year Final Research Report

• Project/Area Number: 25440071
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Biophysics
• Research Institution: Kobe University
• Principal Investigator: Chatani Eri 神戸大学, 理学(系)研究科(研究院), 准教授 (00432493)
• Project Period (FY): 2013-04-01 – 2016-03-31
• Keywords: 蛋白質 / フォールディング / ミスフォールディング / アミロイド線維 / 中間体 / インスリン / 伝播性

Outline of Final Research Achievements

Amyloid fibrils are a form of protein aggregates associated with numerous diseases. One of the most unique and essential properties is their ability to self-propagate, which leads to the explosive amplification of amyloid fibrils and then the onset of the diseases; however, much remains to be elucidated regarding its molecular details how and when the propagating nuclei initially emerge.
In this study, we have trapped and characterized structural properties of prefibrillar intermediate species of insulin and an insulin-derived short peptide, and as for insulin, we have clarified time-dependent formation and evolution of the prefibrillar intermediates by time-resolved small angle X-ray scattering measurement. We also performed time-resolved NIR spectral measurement to clarify more details of the water molecular system dynamics during the nucleation.

Free Research Field

生物学