Entropy of water and the temperature-induced stiffening of amyloid networks

In water, networks of semi-flexible fibrils of the protein \(\alpha\)-synuclein stiffen significantly with increasing temperature. We make plausible that this reversible stiffening is a result of hydrophobic contacts between the fibrils that become more prominent with increasing temperature. The goo...

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Bibliographic Details
Published inarXiv.org
Main Authors Semerdzhiev, Slav A, Lindhoud, Saskia, Stefanovic, Anja, Subramaniam, Vinod, van der Schoot, Paul, Mireille M A E Claessens
Format Paper Journal Article
LanguageEnglish
Published Ithaca Cornell University Library, arXiv.org 20.12.2017
Subjects
Crosslinking
Elasticity
Enthalpy
Hydrophobicity
Physics - Soft Condensed Matter
Proteins
Stiffening
Storage modulus
Temperature
Temperature dependence
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Summary:In water, networks of semi-flexible fibrils of the protein \(\alpha\)-synuclein stiffen significantly with increasing temperature. We make plausible that this reversible stiffening is a result of hydrophobic contacts between the fibrils that become more prominent with increasing temperature. The good agreement of our experimentally observed temperature dependence of the storage modulus of the network with a scaling theory linking network elasticity with reversible crosslinking enables us to quantify the endothermic binding enthalpy and an estimate the effective size of hydrophobic patches on the fibril surface.
ISSN:2331-8422
DOI:10.48550/arxiv.1712.07674