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:info:doi/10.1074/jbc.M111.226688

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論文情報

タイトル	Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions
著者	Yanagi, Kotaro Yanagi, Kotaro
	Ashizaki, Mizue Ashizaki, Mizue
	Yagi, Hisashi Yagi, Hisashi
	Sakurai, Kazumasa Sakurai, Kazumasa
	Lee, Young-Ho Lee, Young-Ho
	Goto, Yuji 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.
公開者	American Society for Biochemistry and Molecular Biology
掲載誌名	Journal of Biological Chemistry
巻	286
号	27
開始ページ	23959
終了ページ	23966
刊行年月	2011-07
ISSN	1083351X
NCID	AA1202452X
DOI	info:doi/10.1074/jbc.M111.226688
URL	http://hdl.handle.net/11094/71283
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	Journal of Biological Chemistry.286(27) P.23959-P.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
DCTERMS.issued" scheme="DCTERMS.W3CDTF	2011-07
DC.identifier	info:doi/10.1074/jbc.M111.226688
DC.identifier" scheme="DCTERMS.URI	http://hdl.handle.net/11094/71283
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.
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_issn	1083351X
citation_doi	info:doi/10.1074/jbc.M111.226688
citation_public_url	http://hdl.handle.net/11094/71283

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