SEMINAR

Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson’s disease patients

Abstract
Lewy bodies, which mainly consist of α-synuclein, are neuropathological hallmarks of patients with Parkinson's disease. The fine structure of Lewy bodies is unknown, and Lewy bodies cannot be made artificially. Nevertheless, many studies have described fibrillisation using recombinant α-synuclein purified from E. coli. An extremely fundamental problem is whether the structure of Lewy bodies is the same as that of recombinant amyloid fibrils. Thus, we used synchrotron Fourier transform infrared micro-spectroscopy to analyse the fine structure of Lewy bodies in the brain of a Parkinson’s disease patient. Our results showed that Lewy bodies have a β-sheet-rich structure. A 2D mapping study of Lewy bodies revealed that the contents of the β-sheet structure are higher in the halo than in the core, whereas the core contains large amounts of proteins and lipids. This is the first in-depth presentation of the detailed structure of Lewy bodies with synchrotron Fourier transform infrared micro-spectroscopy.

BIOGRAPHY

2011-present: Clinical Fellow, Department of Neurology, Osaka University Graduate School of Medicine
2009-2011: Resident, Toyonaka Municipal Hospital
2007-2009: Resident, Ikeda Municipal Hospital
2007: M.D., Faculty of Medicine, Osaka University
1998: B.Sc., Faculty of Science (Physics), Kyoto University

Research Fields and Interests:

I am interested in the pathogenesis of and treatment for Parkinson's disease. We perform a structural analysis for α-synuclein and the Lewy bodies of autopsy human brain at SPring-8. In a collaborative research with Goto laboratory, we are developing methods for the diagnosis of Parkinson's disease and screening of aggregation inhibitor by HANABI.