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

Norrild, Rasmus K., Vettore, Nicola, Coden, Alberto, Xue, Wei-Feng, Buell, Alexander K. (2021) Thermodynamics of amyloid fibril formation from non-equilibrium experiments of growth and dissociation. Biophysical Chemistry, 271 . p. 106549. ISSN 0301-4622. (doi:10.1016/j.bpc.2021.106549) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:93216)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)
Official URL:
https://doi.org/10.1016/j.bpc.2021.106549

Abstract

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.

Item Type: Article
DOI/Identification number: 10.1016/j.bpc.2021.106549
Uncontrolled keywords: Amyloid Kinetics Thermodynamics Non-equilibrium system Biosensing Differential scanning fluorimetry Quartz crystal microbalance
Subjects: Q Science
Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Wei-Feng Xue
Date Deposited: 16 Feb 2022 14:50 UTC
Last Modified: 18 Feb 2022 19:35 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/93216 (The current URI for this page, for reference purposes)

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