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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.
- This article is part of the themed collections: Amyloids and Protein Aggregation, Most popular 2022 chemical biology articles, 2022 ChemSci Pick of the Week Collection, 2022 Chemical Science Perspective & Review Collection and 2022 Chemical Science HOT Article Collection
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