Thermodynamics of amyloid fibril formation from non-equilibrium experiments of growth and dissociation

Amyloid fibrils are ordered, non-covalent polymers of proteins that are linked to a range of diseases, as well as biological functions. Amyloid fibrils are often considered thermodynamically so stable that they appear to be irreversible, explaining why very few quantitative thermodynamic studies hav...

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Published inBiophysical chemistry Vol. 271; p. 106549
Main Authors Norrild, Rasmus K., Vettore, Nicola, Coden, Alberto, Xue, Wei-Feng, Buell, Alexander K.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.04.2021
Subjects
Amyloid
Amyloid - biosynthesis
Amyloid - chemistry
Biosensing
Differential scanning fluorimetry
Fluorometry
Kinetics
Non-equilibrium system
Quartz crystal microbalance
Quartz Crystal Microbalance Techniques
Thermodynamics
Thermodynamics
Non-equilibrium system
Amyloid
Kinetics
Quartz crystal microbalance
Differential scanning fluorimetry
Biosensing
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Summary:Amyloid fibrils are ordered, non-covalent polymers of proteins that are linked to a range of diseases, as well as biological functions. Amyloid fibrils are often considered thermodynamically so stable that they appear to be irreversible, explaining why very few quantitative thermodynamic studies have been performed on amyloid fibrils, compared to the very large body of kinetic studies. Here we explore the thermodynamics of amyloid fibril formation by the protein PI3K-SH3, which forms amyloid fibrils under acidic conditions. We use quartz crystal microbalance (QCM) and develop novel temperature perturbation experiments based on differential scanning fluorimetry (DSF) to measure the temperature dependence of the fibril growth and dissociation rates, allowing us to quantitatively describe the thermodynamic stability of PI3K-SH3 amyloid fibrils between 10 and 75°C. [Display omitted] •A novel differential scanning fluorimetry method to characterise amyloid fibril growth and dissociation kinetics•Determination of full thermodynamics of an amyloid system over a wide temperature range•Thermodynamic stability from kinetic experiments in good agreement with equilibrium depolymerisation•Temperature jump and temperature ramp experiments of amyloid fibrils
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ISSN:0301-4622
1873-4200
DOI:10.1016/j.bpc.2021.106549