Supersaturation-limited and unlimited phase transitions compete to produce the pathway complexity in amyloid fibrillation

Adachi, Masayuki; So, Masatomo; Sakura, Kazumasa; Kardos, József; Goto, Yuji

doi:https://doi.org/10.1074/jbc.M115.648139

Supersaturation-limited and unlimited phase transitions compete to produce the pathway complexity in amyloid fibrillation

Adachi, Masayuki; So, Masatomo; Sakura, Kazumasa et al.

Journal of Biological Chemistry, 2015, 290(29), 18134-18145

アクセス数:582件（2025-07-07 15:59 集計）

固定URL: https://hdl.handle.net/11094/71273

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タイトル	Supersaturation-limited and unlimited phase transitions compete to produce the pathway complexity in amyloid fibrillation
著者	著者名 Adachi, Masayuki
	NRID 1000040746335 1000040746335 著者名 So, Masatomo
	著者名 Sakura, Kazumasa
	著者名 Kardos, József
	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. Masayuki Adachi, Masatomo So, Kazumasa Sakura, József Kardos and Yuji Goto. Supersaturation-limited and Unlimited Phase Transitions Compete to Produce the Pathway Complexity in Amyloid Fibrillation. J. Biol. Chem. 2015; 290, 18134-18145. © the American Society for Biochemistry and Molecular Biology
抄録	Although amyloid fibrils and amorphous aggregates are two types of aggregates formed by denatured proteins, their relationship currently remains unclear. We used β2-microglobulin (β2m), a protein responsible for dialysis-related amyloidosis, to clarify the mechanism by which proteins form either amyloid fibrils or amorphous aggregates. When ultrasonication was used to accelerate the spontaneous fibrillation of β2m at pH 2.0, the effects observed depended on ultrasonic power; although stronger ultrasonic power effectively accelerated fibrillation, excessively strong ultrasonic power decreased the amount of fibrils formed, as monitored by thioflavin T fluorescence. An analysis of the products formed indicated that excessively strong ultrasonic power generated fibrillar aggregates that retained β-structures but without high efficiency as seeds. On the other hand, when the spontaneous fibrillation of β2m was induced at higher concentrations of NaCl at pH 2.0 with stirring, amorphous aggregates became more dominant than amyloid fibrils. These apparent complexities in fibrillation were explained comprehensively by a competitive mechanism in which supersaturation-limited reactions competed with supersaturation-unlimited reactions. We link the kinetics of protein aggregation and a conformational phase diagram, in which supersaturation played important roles.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	290(29)
ページ	18134-18145
刊行年月	2015-06
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71273
eISSN	1083351X
NCID	AA1202442X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M115.648139
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. 2015, 290(29), p. 18134-18145
DC.title	Supersaturation-limited and unlimited phase transitions compete to produce the pathway complexity in amyloid fibrillation
DC.creator	Adachi, Masayuki
	So, Masatomo
	Sakura, Kazumasa
	Kardos, József
	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	2015-06
DC.identifier	https://doi.org/10.1074/jbc.M115.648139
DC.description	This research was originally published in the Journal of Biological Chemistry. Masayuki Adachi, Masatomo So, Kazumasa Sakura, József Kardos and Yuji Goto. Supersaturation-limited and Unlimited Phase Transitions Compete to Produce the Pathway Complexity in Amyloid Fibrillation. J. Biol. Chem. 2015; 290, 18134-18145. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	Although amyloid fibrils and amorphous aggregates are two types of aggregates formed by denatured proteins, their relationship currently remains unclear. We used β2-microglobulin (β2m), a protein responsible for dialysis-related amyloidosis, to clarify the mechanism by which proteins form either amyloid fibrils or amorphous aggregates. When ultrasonication was used to accelerate the spontaneous fibrillation of β2m at pH 2.0, the effects observed depended on ultrasonic power; although stronger ultrasonic power effectively accelerated fibrillation, excessively strong ultrasonic power decreased the amount of fibrils formed, as monitored by thioflavin T fluorescence. An analysis of the products formed indicated that excessively strong ultrasonic power generated fibrillar aggregates that retained β-structures but without high efficiency as seeds. On the other hand, when the spontaneous fibrillation of β2m was induced at higher concentrations of NaCl at pH 2.0 with stirring, amorphous aggregates became more dominant than amyloid fibrils. These apparent complexities in fibrillation were explained comprehensively by a competitive mechanism in which supersaturation-limited reactions competed with supersaturation-unlimited reactions. We link the kinetics of protein aggregation and a conformational phase diagram, in which supersaturation played important roles.
DC.format	71273
citation_title	Supersaturation-limited and unlimited phase transitions compete to produce the pathway complexity in amyloid fibrillation
citation_author	Adachi, Masayuki
	So, Masatomo
	Sakura, Kazumasa
	Kardos, József
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2015-06
citation_journal_title	Journal of Biological Chemistry
citation_volume	290
citation_issue	29
citation_firstpage	18134
citation_lastpage	18145
citation_doi	https://doi.org/10.1074/jbc.M115.648139
citation_public_url	https://hdl.handle.net/11094/71273

Supersaturation-limited and unlimited phase transitions compete to produce the pathway complexity in amyloid fibrillation

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