Investigation of a Peptide Responsible for Amyloid Fibril Formation of β2-Microglobulin by Achromobacter Protease I

Kozhukh, Gennady V.; Hagihara, Yoshihisa; Kawakami, Toru; Hasegawa, Kazuhiro; Naiki, Hironobu; Goto, Yuji

doi:info:doi/10.1074/jbc.M108753200

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タイトル	Investigation of a Peptide Responsible for Amyloid Fibril Formation of β2-Microglobulin by Achromobacter Protease I
著者	Kozhukh, Gennady V. Kozhukh, Gennady V.
	Hagihara, Yoshihisa Hagihara, Yoshihisa
	Kawakami, Toru Kawakami, Toru
	Hasegawa, Kazuhiro Hasegawa, Kazuhiro
	Naiki, Hironobu Naiki, Hironobu
	Goto, Yuji Goto, Yuji
内容	This research was originally published in the Journal of Biological Chemistry. Gennady V. Kozhukh, Yoshihisa Hagihara, Toru Kawakami, Kazuhiro Hasegawa, Hironobu Naiki and Yuji Goto. Investigation of a Peptide Responsible for Amyloid Fibril Formation of β2-Microglobulin by Achromobacter Protease I. J. Biol. Chem. 2002; 277, 1310-1315. © the American Society for Biochemistry and Molecular Biology
抄録	To obtain insight into the mechanism of amyloid fibril formation from β2-microglobulin (β2-m), we prepared a series of peptide fragments using a lysine-specific protease from Achromobacter lyticus and examined their ability to form amyloid fibrils at pH 2.5. Among the nine peptides prepared by the digestion, the peptide Ser20–Lys41 (K3) spontaneously formed amyloid fibrils, confirmed by thioflavin T binding and electron microscopy. The fibrils composed of K3 peptide induced fibril formation of intact β2-m with a lag phase, distinct from the extension reaction without a lag phase observed for intact β2-m seeds. Fibril formation of K3 peptide with intact β2-m seeds also exhibited a lag phase. On the other hand, the extension reaction of K3 peptide with the K3 seeds occurred without a lag phase. At neutral pH, the fibrils composed of either intact β2-m or K3 peptide spontaneously depolymerized. Intriguingly, the depolymerization of K3 fibrils was faster than that of intact β2-m fibrils. These results indicated that, although K3 peptide can form fibrils by itself more readily than intact β2-m, the K3 fibrils are less stable than the intact β2-m fibrils, suggesting a close relation between the free energy barrier of amyloid fibril formation and its stability.
公開者	American Society for Biochemistry and Molecular Biology
掲載誌名	Journal of Biological Chemistry
巻	277
号	2
開始ページ	1310
終了ページ	1315
刊行年月	2002-01
ISSN	1083351X
NCID	AA1202473X
DOI	info:doi/10.1074/jbc.M108753200
URL	http://hdl.handle.net/11094/71304
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.277(2) P.1310-P.1315
DC.title	Investigation of a Peptide Responsible for Amyloid Fibril Formation of β2-Microglobulin by Achromobacter Protease I
DC.creator	Kozhukh, Gennady V.
	Hagihara, Yoshihisa
	Kawakami, Toru
	Hasegawa, Kazuhiro
	Naiki, Hironobu
	Goto, Yuji
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language" scheme="DCTERMS.RFC1766	英語
DCTERMS.issued" scheme="DCTERMS.W3CDTF	2002-01
DC.identifier	info:doi/10.1074/jbc.M108753200
DC.identifier" scheme="DCTERMS.URI	http://hdl.handle.net/11094/71304
DC.description	This research was originally published in the Journal of Biological Chemistry. Gennady V. Kozhukh, Yoshihisa Hagihara, Toru Kawakami, Kazuhiro Hasegawa, Hironobu Naiki and Yuji Goto. Investigation of a Peptide Responsible for Amyloid Fibril Formation of β2-Microglobulin by Achromobacter Protease I. J. Biol. Chem. 2002; 277, 1310-1315. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	To obtain insight into the mechanism of amyloid fibril formation from β2-microglobulin (β2-m), we prepared a series of peptide fragments using a lysine-specific protease from Achromobacter lyticus and examined their ability to form amyloid fibrils at pH 2.5. Among the nine peptides prepared by the digestion, the peptide Ser20–Lys41 (K3) spontaneously formed amyloid fibrils, confirmed by thioflavin T binding and electron microscopy. The fibrils composed of K3 peptide induced fibril formation of intact β2-m with a lag phase, distinct from the extension reaction without a lag phase observed for intact β2-m seeds. Fibril formation of K3 peptide with intact β2-m seeds also exhibited a lag phase. On the other hand, the extension reaction of K3 peptide with the K3 seeds occurred without a lag phase. At neutral pH, the fibrils composed of either intact β2-m or K3 peptide spontaneously depolymerized. Intriguingly, the depolymerization of K3 fibrils was faster than that of intact β2-m fibrils. These results indicated that, although K3 peptide can form fibrils by itself more readily than intact β2-m, the K3 fibrils are less stable than the intact β2-m fibrils, suggesting a close relation between the free energy barrier of amyloid fibril formation and its stability.
citation_title	Investigation of a Peptide Responsible for Amyloid Fibril Formation of β2-Microglobulin by Achromobacter Protease I
citation_author	Kozhukh, Gennady V.
	Hagihara, Yoshihisa
	Kawakami, Toru
	Hasegawa, Kazuhiro
	Naiki, Hironobu
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2002-01
citation_journal_title	Journal of Biological Chemistry
citation_volume	277
citation_issue	2
citation_firstpage	1310
citation_lastpage	1315
citation_issn	1083351X
citation_doi	info:doi/10.1074/jbc.M108753200
citation_public_url	http://hdl.handle.net/11094/71304

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