Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry

J. Kardos, Kaori Yamamoto, Kazuhiro Hasegawa, Hironobu Naiki, Yuji Goto

Research output: Contribution to journalArticle

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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.

Original languageEnglish
Pages (from-to)55308-55314
Number of pages7
JournalJournal of Biological Chemistry
Volume279
Issue number53
DOIs
Publication statusPublished - Dec 31 2004

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Calorimetry
Titration
Thermodynamics
Amyloid
Specific heat
Enthalpy
Hot Temperature
Burial
Prion Diseases
Dialysis
Prions
Amyloidosis
Calorimeters
Parkinson Disease
Seed
Seeds
Alzheimer Disease
Molecules
Acids

ASJC Scopus subject areas

  • Biochemistry

Cite this

Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry. / Kardos, J.; Yamamoto, Kaori; Hasegawa, Kazuhiro; Naiki, Hironobu; Goto, Yuji.

In: Journal of Biological Chemistry, Vol. 279, No. 53, 31.12.2004, p. 55308-55314.

Research output: Contribution to journalArticle

Kardos, J. ; Yamamoto, Kaori ; Hasegawa, Kazuhiro ; Naiki, Hironobu ; Goto, Yuji. / Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry. In: Journal of Biological Chemistry. 2004 ; Vol. 279, No. 53. pp. 55308-55314.
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