Application and use of differential scanning calorimetry in studies of thermal fluctuation associated with amyloid fibril formation

Biophysics Reviews
Kenji Sasahara, Yuji Goto

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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Jun 21, 2017·Chemical Communications : Chem Comm·A M GarciaS Marchesan
Dec 23, 2016·Biophysics Reviews·Ran ZhaoDamien Hall
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May 20, 2015·Biomacromolecules·Rita GuzziMaria P De Santo
Jun 28, 2019·The Journal of Physical Chemistry. B·Goutam GhoshSuhrit Ghosh

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