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

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

doi:https://doi.org/10.1074/jbc.M409677200

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

Kardos, József; Yamamoto, Kaori; Hasegawa, Kazuhiro et al.

Journal of Biological Chemistry, 2004, 279(53), 55308-55314

アクセス数:671件（2025-07-11 19:39 集計）

固定URL: https://hdl.handle.net/11094/71296

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タイトル	Direct Measurement of the Thermodynamic Parameters of Amyloid Formation by Isothermal Titration Calorimetry
著者	著者名 Kardos, József
	著者名 Yamamoto, Kaori
	NRID 1000060324159 1000060324159 著者名 Hasegawa, Kazuhiro
	NRID 1000010227704 1000010227704 著者名 Naiki, Hironobu
	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. 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.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	279(53)
ページ	55308-55314
刊行年月	2004-12
言語	英語
ハンドルURL	https://hdl.handle.net/11094/71296
eISSN	1083351X
NCID	AA1202465X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M409677200
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. 2004, 279(53), p. 55308-55314
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
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2004-12
DC.identifier	https://doi.org/10.1074/jbc.M409677200
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.
DC.format	71296
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_doi	https://doi.org/10.1074/jbc.M409677200
citation_public_url	https://hdl.handle.net/11094/71296

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

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