Supersaturation-limited amyloid fibrillation of insulin revealed by ultrasonication

Muta, Hiroya; Lee, Young-Ho; Kardos, József; Lin, Yuxi; Yagi, Hisashi; Goto, Yuji

doi:https://doi.org/10.1074/jbc.M114.566950

アクセス数:229件（2024-09-11 13:40 集計）

固定URL: https://hdl.handle.net/11094/71277

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タイトル	Supersaturation-limited amyloid fibrillation of insulin revealed by ultrasonication
著者	著者名 Muta, Hiroya
	NRID 1000070589431 1000070589431 著者名 Lee, Young-Ho
	著者名 Kardos, József
	著者名 Lin, Yuxi
	NRID 1000010432494 1000010432494 著者名 Yagi, Hisashi
	NRID 1000040153770 1000040153770 researchmap permalink read0014440 read0014440 著者名 Goto, Yuji
内容	This research was originally published in the Journal of Biological Chemistry. Hiroya Muta, Young-Ho Lee, József Kardos, Yuxi Lin, Hisashi Yagi and Yuji Goto. Supersaturation-limited Amyloid Fibrillation of Insulin Revealed by Ultrasonication. J. Biol. Chem. 2014; 289, 18228–18238. © the American Society for Biochemistry and Molecular Biology
抄録	Amyloid fibrils form in supersaturated solutions via a nucleation and growth mechanism. We proposed that ultrasonication may be an effective agitation to trigger nucleation that would otherwise not occur under the persistent metastability of supersaturation. However, the roles of supersaturation and effects of ultrasonication have not been elucidated in detail except for limited cases. Insulin is an amyloidogenic protein that is useful for investigating the mechanisms underlying amyloid fibrillation with biological relevance. We studied the alcohol-induced amyloid fibrillation of insulin using various concentrations of 2,2,2-trifluoroethanol and 1,1,1,3,3,3-hexafluoro-2-propanol at pH 2.0 and 4.8. Ultrasonic irradiation effectively triggered fibrillation under conditions in which insulin retained persistent supersaturation. Structural analyses by circular dichroism, Fourier transform infrared spectroscopy, transmission electron microscopy, and atomic force microscopy revealed that the dominant structures of fibrils varied between parallel and antiparallel β-sheets depending on the solvent conditions. pH and alcohol concentration-dependent phase diagrams showed a marked difference before and after the ultrasonic treatment, which indicated that the persistent metastability of supersaturation determined the conformations of insulin. These results indicate the importance of an alternative view of amyloid fibrils as supersaturation-limited crystal-like aggregates formed above the solubility limit.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	289(26)
ページ	18228-18238
刊行年月	2014-06
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71277
eISSN	1083351X
NCID	AA1202446X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M114.566950
アクセス権	open access
出版タイプ	Version of Record
カテゴリ	学術雑誌論文 Journal Article

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	Journal of Biological Chemistry. 2014, 289(26), p. 18228-18238
DC.title	Supersaturation-limited amyloid fibrillation of insulin revealed by ultrasonication
DC.creator	Muta, Hiroya
	Lee, Young-Ho
	Kardos, József
	Lin, Yuxi
	Yagi, Hisashi
	Goto, Yuji
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2014-06
DC.identifier	https://doi.org/10.1074/jbc.M114.566950
DC.description	This research was originally published in the Journal of Biological Chemistry. Hiroya Muta, Young-Ho Lee, József Kardos, Yuxi Lin, Hisashi Yagi and Yuji Goto. Supersaturation-limited Amyloid Fibrillation of Insulin Revealed by Ultrasonication. J. Biol. Chem. 2014; 289, 18228–18238. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	Amyloid fibrils form in supersaturated solutions via a nucleation and growth mechanism. We proposed that ultrasonication may be an effective agitation to trigger nucleation that would otherwise not occur under the persistent metastability of supersaturation. However, the roles of supersaturation and effects of ultrasonication have not been elucidated in detail except for limited cases. Insulin is an amyloidogenic protein that is useful for investigating the mechanisms underlying amyloid fibrillation with biological relevance. We studied the alcohol-induced amyloid fibrillation of insulin using various concentrations of 2,2,2-trifluoroethanol and 1,1,1,3,3,3-hexafluoro-2-propanol at pH 2.0 and 4.8. Ultrasonic irradiation effectively triggered fibrillation under conditions in which insulin retained persistent supersaturation. Structural analyses by circular dichroism, Fourier transform infrared spectroscopy, transmission electron microscopy, and atomic force microscopy revealed that the dominant structures of fibrils varied between parallel and antiparallel β-sheets depending on the solvent conditions. pH and alcohol concentration-dependent phase diagrams showed a marked difference before and after the ultrasonic treatment, which indicated that the persistent metastability of supersaturation determined the conformations of insulin. These results indicate the importance of an alternative view of amyloid fibrils as supersaturation-limited crystal-like aggregates formed above the solubility limit.
DC.format	71277
citation_title	Supersaturation-limited amyloid fibrillation of insulin revealed by ultrasonication
citation_author	Muta, Hiroya
	Lee, Young-Ho
	Kardos, József
	Lin, Yuxi
	Yagi, Hisashi
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2014-06
citation_journal_title	Journal of Biological Chemistry
citation_volume	289
citation_issue	26
citation_firstpage	18228
citation_lastpage	18238
citation_doi	https://doi.org/10.1074/jbc.M114.566950
citation_public_url	https://hdl.handle.net/11094/71277

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