Journal Title
Title of Journal: Biophys Rev
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Abbravation: Biophysical Reviews
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Publisher
Springer Berlin Heidelberg
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Authors: Kenji Sasahara Yuji Goto
Publish Date: 2012/11/13
Volume: 5, Issue: 3, Pages: 259-269
Abstract
The aggregation of proteins into amyloid fibrils is a topic that has attracted great interest because the process is associated with the pathology of numerous human diseases Despite considerable progress in the elucidation of the structure of amyloid fibrils and the kinetic mechanism of their formation knowledge on the thermodynamic aspects underlying the formation and stability of amyloid fibrils is limited In this review we summarize recent calorimetric studies of amyloid fibril formation with the goal of obtaining a better understanding of the causal factors that thermally induce proteins to aggregate into amyloid fibrils Calorimetric data show that differential scanning calorimetry is a useful technique to study the causative factors that thermally trigger the conversion to the amyloid structure and highlight the physics related to the thermal fluctuation of proteins during this conversion
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