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

Araki, Katsuya; Yagi, Naoto; Ikemoto, Yuka; Yagi, Hisashi; Choong, Chi-Jing; Hayakawa, Hideki; Beck, Goichi; Sumi, Hisae; Fujimura, Harutoshi; Moriwaki, Taro; Nagai, Yoshitaka; Goto, Yuji; Mochizuki, Hideki

doi:info:doi/10.1038/srep17625

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タイトル	Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson’s disease patients
著者	Araki, Katsuya Araki, Katsuya
	Yagi, Naoto Yagi, Naoto
	Ikemoto, Yuka Ikemoto, Yuka
	Yagi, Hisashi Yagi, Hisashi
	Choong, Chi-Jing Choong, Chi-Jing
	Hayakawa, Hideki Hayakawa, Hideki
	Beck, Goichi Beck, Goichi
	Sumi, Hisae Sumi, Hisae
	Fujimura, Harutoshi Fujimura, Harutoshi
	Moriwaki, Taro Moriwaki, Taro
	Nagai, Yoshitaka Nagai, Yoshitaka
	Goto, Yuji Goto, Yuji
	Mochizuki, Hideki Mochizuki, Hideki
内容	Katsuya Araki, Naoto Yagi, Yuka Ikemoto, Hisashi Yagi, Chi-Jing Choong, Hideki Hayakawa, Goichi Beck, Hisae Sumi, Harutoshi Fujimura, Taro Moriwaki, Yoshitaka Nagai, Yuji Goto & Hideki Mochizuki "Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson’s disease patients", Scientific Reports, volume 5, Article number: 17625, Springer Nature, 2015
抄録	Lewy bodies (LBs), which mainly consist of α-synuclein (α-syn), are neuropathological hallmarks of patients with Parkinson’s disease (PD). The fine structure of LBs is unknown, and LBs cannot be made artificially. Nevertheless, many studies have described fibrillisation using recombinant α-syn purified from E. coli. An extremely fundamental problem is whether the structure of LBs is the same as that of recombinant amyloid fibrils. Thus, we used synchrotron Fourier transform infrared micro-spectroscopy (FTIRM) to analyse the fine structure of LBs in the brain of PD patients. Our results showed a shift in the infrared spectrum that indicates abundance of a β-sheet-rich structure in LBs. Also, 2D infrared mapping of LBs revealed that the content of the β-sheet structure is higher in the halo than in the core, and the core contains a large amount of proteins and lipids.
公開者	Springer Nature
掲載誌名	Scientific Reports
巻	5
開始ページ	17625
刊行年月	2015-12
ISSN	20452322
DOI	info:doi/10.1038/srep17625
URL	http://hdl.handle.net/11094/71268
権利情報	This article is licensed under a Creative Commons Attribution 4.0 International License.
言語	英語
カテゴリ	学術雑誌論文 Journal Article

著者版フラグ	publisher
NII資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
dcmi資源タイプ	text
DCTERMS.bibliographicCitation	Scientific Reports.5 P.17625
DC.title	Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson’s disease patients
DC.creator	Araki, Katsuya
	Yagi, Naoto
	Ikemoto, Yuka
	Yagi, Hisashi
	Choong, Chi-Jing
	Hayakawa, Hideki
	Beck, Goichi
	Sumi, Hisae
	Fujimura, Harutoshi
	Moriwaki, Taro
	Nagai, Yoshitaka
	Goto, Yuji
	Mochizuki, Hideki
DC.publisher	Springer Nature
DC.language" scheme="DCTERMS.RFC1766	英語
DCTERMS.issued" scheme="DCTERMS.W3CDTF	2015-12
DC.identifier	info:doi/10.1038/srep17625
DC.identifier" scheme="DCTERMS.URI	http://hdl.handle.net/11094/71268
DC.description	Katsuya Araki, Naoto Yagi, Yuka Ikemoto, Hisashi Yagi, Chi-Jing Choong, Hideki Hayakawa, Goichi Beck, Hisae Sumi, Harutoshi Fujimura, Taro Moriwaki, Yoshitaka Nagai, Yuji Goto & Hideki Mochizuki "Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson’s disease patients", Scientific Reports, volume 5, Article number: 17625, Springer Nature, 2015
DCTERMS.abstract	Lewy bodies (LBs), which mainly consist of α-synuclein (α-syn), are neuropathological hallmarks of patients with Parkinson’s disease (PD). The fine structure of LBs is unknown, and LBs cannot be made artificially. Nevertheless, many studies have described fibrillisation using recombinant α-syn purified from E. coli. An extremely fundamental problem is whether the structure of LBs is the same as that of recombinant amyloid fibrils. Thus, we used synchrotron Fourier transform infrared micro-spectroscopy (FTIRM) to analyse the fine structure of LBs in the brain of PD patients. Our results showed a shift in the infrared spectrum that indicates abundance of a β-sheet-rich structure in LBs. Also, 2D infrared mapping of LBs revealed that the content of the β-sheet structure is higher in the halo than in the core, and the core contains a large amount of proteins and lipids.
DC.rights	This article is licensed under a Creative Commons Attribution 4.0 International License.
citation_title	Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson’s disease patients
citation_author	Araki, Katsuya
	Yagi, Naoto
	Ikemoto, Yuka
	Yagi, Hisashi
	Choong, Chi-Jing
	Hayakawa, Hideki
	Beck, Goichi
	Sumi, Hisae
	Fujimura, Harutoshi
	Moriwaki, Taro
	Nagai, Yoshitaka
	Goto, Yuji
	Mochizuki, Hideki
citation_publisher	Springer Nature
citation_language	英語
citation_date	2015-12
citation_journal_title	Scientific Reports
citation_volume	5
citation_firstpage	17625
citation_issn	20452322
citation_doi	info:doi/10.1038/srep17625
citation_public_url	http://hdl.handle.net/11094/71268

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