Direct Measurement of the Thermodynamic Parameters of Amyloid Formation by Isothermal Titration Calorimetry

Kardos, József; Yamamoto, Kaori; Hasegawa, Kazuhiro; Naiki, Hironobu; Goto, Yuji

doi:info:doi/10.1074/jbc.M409677200

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タイトル	Direct Measurement of the Thermodynamic Parameters of Amyloid Formation by Isothermal Titration Calorimetry
著者	Kardos, József Kardos, József
	Yamamoto, Kaori Yamamoto, Kaori
	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. József Kardos, Kaori Yamamoto, Kazuhiro Hasegawa, Hironobu Naiki and Yuji Goto. Direct Measurement of the Thermodynamic Parameters of Amyloid Formation by Isothermal Titration Calorimetry. J. Biol. Chem. 2004; 279, 55308-55314. © the American Society for Biochemistry and Molecular Biology
抄録	Amyloid fibril deposition is associated with over 20 degenerative diseases, including Alzheimer's, Parkinson's, and prion diseases. Although research over the last few years has revealed the morphology and structural features of the amyloid form, knowledge about the thermodynamics of amyloid formation is limited. Here, we report for the first time a direct thermodynamic study of amyloid formation using isothermal titration calorimetry. β2-Microglobulin, a protein responsible for dialysis-related amyloidosis, was used for extending amyloid fibrils in a seed-controlled reaction in the cell of the calorimeter. We investigated the enthalpy and heat capacity changes of the reaction, where the monomeric, acid-denatured molecules adopt an ordered, cross-β-sheet structure in the rigid amyloid fibrils. Despite the dramatic difference in morphology, β2-microglobulin exhibited a similar heat capacity change upon amyloid formation to that of the folding to the native globular state, whereas the enthalpy change of the reaction proved to be markedly lower. In comparison with the native state, the results outline the important structural features of the amyloid fibrils: a similar extent of surface burial even with the supramolecular architecture of amyloid fibrils, a lower level of internal packing, and the possible presence of unfavorable side chain contributions.
公開者	American Society for Biochemistry and Molecular Biology
掲載誌名	Journal of Biological Chemistry
巻	279
号	53
開始ページ	55308
終了ページ	55314
刊行年月	2004-12
ISSN	1083351X
NCID	AA1202465X
DOI	info:doi/10.1074/jbc.M409677200
URL	http://hdl.handle.net/11094/71296
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.279(53) P.55308-P.55314
DC.title	Direct Measurement of the Thermodynamic Parameters of Amyloid Formation by Isothermal Titration Calorimetry
DC.creator	Kardos, József
	Yamamoto, Kaori
	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	2004-12
DC.identifier	info:doi/10.1074/jbc.M409677200
DC.identifier" scheme="DCTERMS.URI	http://hdl.handle.net/11094/71296
DC.description	This research was originally published in the Journal of Biological Chemistry. József Kardos, Kaori Yamamoto, Kazuhiro Hasegawa, Hironobu Naiki and Yuji Goto. Direct Measurement of the Thermodynamic Parameters of Amyloid Formation by Isothermal Titration Calorimetry. J. Biol. Chem. 2004; 279, 55308-55314. © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	Amyloid fibril deposition is associated with over 20 degenerative diseases, including Alzheimer's, Parkinson's, and prion diseases. Although research over the last few years has revealed the morphology and structural features of the amyloid form, knowledge about the thermodynamics of amyloid formation is limited. Here, we report for the first time a direct thermodynamic study of amyloid formation using isothermal titration calorimetry. β2-Microglobulin, a protein responsible for dialysis-related amyloidosis, was used for extending amyloid fibrils in a seed-controlled reaction in the cell of the calorimeter. We investigated the enthalpy and heat capacity changes of the reaction, where the monomeric, acid-denatured molecules adopt an ordered, cross-β-sheet structure in the rigid amyloid fibrils. Despite the dramatic difference in morphology, β2-microglobulin exhibited a similar heat capacity change upon amyloid formation to that of the folding to the native globular state, whereas the enthalpy change of the reaction proved to be markedly lower. In comparison with the native state, the results outline the important structural features of the amyloid fibrils: a similar extent of surface burial even with the supramolecular architecture of amyloid fibrils, a lower level of internal packing, and the possible presence of unfavorable side chain contributions.
citation_title	Direct Measurement of the Thermodynamic Parameters of Amyloid Formation by Isothermal Titration Calorimetry
citation_author	Kardos, József
	Yamamoto, Kaori
	Hasegawa, Kazuhiro
	Naiki, Hironobu
	Goto, Yuji
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2004-12
citation_journal_title	Journal of Biological Chemistry
citation_volume	279
citation_issue	53
citation_firstpage	55308
citation_lastpage	55314
citation_issn	1083351X
citation_doi	info:doi/10.1074/jbc.M409677200
citation_public_url	http://hdl.handle.net/11094/71296

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