Hydrophobic-Interaction-Induced Stiffening of α -Synuclein Fibril Networks

Slav A. Semerdzhiev, Saskia Lindhoud, Anja Stefanovic, Vinod Subramaniam, Paul Van Der Schoot, Mireille M.A.E. Claessens*

*Corresponding author for this work

    Research output: Contribution to JournalArticleAcademicpeer-review


    In water, networks of semiflexible fibrils of the protein α-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 cross-linking enables us to quantify the endothermic binding enthalpy and estimate the effective size of hydrophobic patches on the fibril surface. Our findings may not only shed light on the role of amyloid deposits in disease conditions, but can also inspire new approaches for the design of thermoresponsive materials.

    Original languageEnglish
    Article number208102
    Pages (from-to)1-6
    Number of pages6
    JournalPhysical Review Letters
    Issue number20
    Publication statusPublished - 17 May 2018


    This work was supported by the Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO) through NWO-CW Veni grant (722.013.013) to S. L., NWO-CW TOP program (700.58.302) to V. S., NWO-CW VIDI grant (700.59.423) to M. M. A. E. C., and through and Nanonext NL theme 8A. The authors thank Kirsten van Leijenhorst-Groener and Nathalie Schilderink for the expression and purification of -synuclein. SAXS experiments were performed at ESRF, BM26 (DUBBLE) experiment no, 26-02-664. We thank Dr. G. Portale (Beamline Scientist) for his help performing SAXS experiments.

    FundersFunder number
    NWO-CW VIDI700.59.423
    NWO-CW Veni722.013.013
    Nanonext NL theme 8A
    Nederlandse Organisatie voor Wetenschappelijk Onderzoek700.58.302


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