Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions

Yanagi, Kotaro; Ashizaki, Mizue; Yagi, Hisashi; Sakurai, Kazumasa; Lee, Young-Ho; Goto, Yuji

doi:https://doi.org/10.1074/jbc.M111.226688

Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions

Yanagi, Kotaro; Ashizaki, Mizue; Yagi, Hisashi et al.

Journal of Biological Chemistry, 2011, 286(27), 23959-23966

アクセス数:680件（2025-07-13 21:15 集計）

固定URL: https://hdl.handle.net/11094/71283

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タイトル	Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions
著者	著者名 Yanagi, Kotaro
	著者名 Ashizaki, Mizue
	NRID 1000010432494 1000010432494 著者名 Yagi, Hisashi
	NRID 1000010403015 1000010403015 著者名 Sakurai, Kazumasa
	NRID 1000070589431 1000070589431 著者名 Lee, Young-Ho
	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. Kotaro Yanagi, Mizue Ashizaki, Hisashi Yagi, Kazumasa Sakurai, Young-Ho Lee and Yuji Goto. Hexafluoroisopropanol Induces Amyloid Fibrils of Islet Amyloid Polypeptide by Enhancing Both Hydrophobic and Electrostatic Interactions. J. Biol. Chem. 2011; 286, 23959-23966. © the American Society for Biochemistry and Molecular Biology
抄録	Although amyloid fibrils deposit with various proteins, the comprehensive mechanism by which they form remains unclear. We studied the formation of fibrils of human islet amyloid polypeptide associated with type II diabetes in the presence of various concentrations of 1,1,1,3,3,3-hexafluoroisopropanol (HFIP) under acidic and neutral pH conditions using CD, amyloid-specific thioflavin T fluorescence, fluorescence imaging with thioflavin T, and atomic force microscopy. At low pH, the formation of fibrils was promoted by HFIP with an optimum at 5% (v/v). At neutral pH in the absence of HFIP, significant amounts of amorphous aggregates formed in addition to the fibrils. The addition of HFIP suppressed the formation of amorphous aggregates, leading to a predominance of fibrils with an optimum effect at 25% (v/v). Under both conditions, higher concentrations of HFIP dissolved the fibrils and stabilized the α-helical structure. The results indicate that fibrils and amorphous aggregates are different types of precipitates formed by exclusion from water-HFIP mixtures. The exclusion occurs through the combined effects of hydrophobic interactions and electrostatic interactions, both of which are strengthened by low concentrations of HFIP, and a subtle balance between the two types of interactions determines whether the fibrils or amorphous aggregates dominate. We suggest a general view of how the structure of precipitates varies dramatically from single crystals to amyloid fibrils and amorphous aggregates.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	286(27)
ページ	23959-23966
刊行年月	2011-07
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71283
eISSN	1083351X
NCID	AA1202452X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M111.226688
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. 2011, 286(27), p. 23959-23966
DC.title	Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions
DC.creator	Yanagi, Kotaro
	Ashizaki, Mizue
	Yagi, Hisashi
	Sakurai, Kazumasa
	Lee, Young-Ho
	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	2011-07
DC.identifier	https://doi.org/10.1074/jbc.M111.226688
DC.description	This research was originally published in the Journal of Biological Chemistry. Kotaro Yanagi, Mizue Ashizaki, Hisashi Yagi, Kazumasa Sakurai, Young-Ho Lee and Yuji Goto. Hexafluoroisopropanol Induces Amyloid Fibrils of Islet Amyloid Polypeptide by Enhancing Both Hydrophobic and Electrostatic Interactions. J. Biol. Chem. 2011; 286, 23959-23966. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	Although amyloid fibrils deposit with various proteins, the comprehensive mechanism by which they form remains unclear. We studied the formation of fibrils of human islet amyloid polypeptide associated with type II diabetes in the presence of various concentrations of 1,1,1,3,3,3-hexafluoroisopropanol (HFIP) under acidic and neutral pH conditions using CD, amyloid-specific thioflavin T fluorescence, fluorescence imaging with thioflavin T, and atomic force microscopy. At low pH, the formation of fibrils was promoted by HFIP with an optimum at 5% (v/v). At neutral pH in the absence of HFIP, significant amounts of amorphous aggregates formed in addition to the fibrils. The addition of HFIP suppressed the formation of amorphous aggregates, leading to a predominance of fibrils with an optimum effect at 25% (v/v). Under both conditions, higher concentrations of HFIP dissolved the fibrils and stabilized the α-helical structure. The results indicate that fibrils and amorphous aggregates are different types of precipitates formed by exclusion from water-HFIP mixtures. The exclusion occurs through the combined effects of hydrophobic interactions and electrostatic interactions, both of which are strengthened by low concentrations of HFIP, and a subtle balance between the two types of interactions determines whether the fibrils or amorphous aggregates dominate. We suggest a general view of how the structure of precipitates varies dramatically from single crystals to amyloid fibrils and amorphous aggregates.
DC.format	71283
citation_title	Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions
citation_author	Yanagi, Kotaro
	Ashizaki, Mizue
	Yagi, Hisashi
	Sakurai, Kazumasa
	Lee, Young-Ho
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2011-07
citation_journal_title	Journal of Biological Chemistry
citation_volume	286
citation_issue	27
citation_firstpage	23959
citation_lastpage	23966
citation_doi	https://doi.org/10.1074/jbc.M111.226688
citation_public_url	https://hdl.handle.net/11094/71283

Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions

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