Investigation of interfaces on protein among aggregate on living cell

2017 Fiscal Year Final Research Report

• Project/Area Number: 15K01804
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Biomolecular chemistry
• Research Institution: Tohoku University
• Principal Investigator: Teruya Kenta 東北大学, 医学系研究科, 准教授 (30372288)
• Project Period (FY): 2015-10-21 – 2018-03-31
• Keywords: プリオン / クロスリンク / 光反応 / 増感剤

Outline of Final Research Achievements

Molecular pathology of prion diseases is characterized by abnormal prion protein (PrPSc), which involves both structural changes at the molecular level and aggregate formation. Understanding of the interface among PrPSc in the aggregate is a core subject in prion. In general, a bis-functionalized crosslinker is used to analyze. Since the normal and abnormal PrP are identical in the denatured state, it is principally difficult to adapt for access the molecule in the fibril. Thus, methods have been required to mark on a protein molecule in the fibril before denaturation.
I found a method that can solve the lemma by a photo-reaction, furthermore, beneficial sensitizers. As results, I established a crosslinking method that is effective in contaminated systems and selective for PrPSc. Also, the method is compatible with purification and a biochemical method for discrimination of PrPSc from normal one. Finally, an anti-body panel indicated the a specific region of PrPSc confer the interface.

Free Research Field

蛋白質化学