Issue 35, 2022

Stability matters, too – the thermodynamics of amyloid fibril formation

Abstract

Amyloid fibrils are supramolecular homopolymers of proteins that play important roles in biological functions and disease. These objects have received an exponential increase in attention during the last few decades, due to their role in the aetiology of a range of severe disorders, most notably some of a neurodegenerative nature. While an overwhelming number of experimental studies exist that investigate how, and how fast, amyloid fibrils form and how their formation can be inhibited, a much more limited body of experimental work attempts to answer the question as to why these types of structures form (i.e. the thermodynamic driving force) and how stable they actually are. In this review, I attempt to give an overview of the types of experiments that have been performed to-date to answer these questions, and to summarise our current understanding of amyloid thermodynamics.

Graphical abstract: Stability matters, too – the thermodynamics of amyloid fibril formation

Article information

Article type
Review Article
Submitted
05 Dec. 2021
Accepted
30 Janv. 2022
First published
02 Febr. 2022
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2022,13, 10177-10192

Stability matters, too – the thermodynamics of amyloid fibril formation

A. K. Buell, Chem. Sci., 2022, 13, 10177 DOI: 10.1039/D1SC06782F

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