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

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Uittreksel

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.

TaalEngels
Artikelnummer208102
TijdschriftPhysical Review Letters
Volume120
Nummer van het tijdschrift20
DOI's
StatusGepubliceerd - 17 mei 2018

Vingerafdruk

stiffening
interactions
elastic properties
enthalpy
deposits
proteins
scaling
temperature dependence
temperature
estimates
water

Citeer dit

Semerdzhiev, S. A., Lindhoud, S., Stefanovic, A., Subramaniam, V., van der Schoot, P., & Claessens, M. M. A. E. (2018). Hydrophobic-interaction-induced stiffening of α -synuclein fibril networks. Physical Review Letters, 120(20), [208102]. DOI: 10.1103/PhysRevLett.120.208102
Semerdzhiev, Slav A. ; Lindhoud, Saskia ; Stefanovic, Anja ; Subramaniam, Vinod ; van der Schoot, Paul ; Claessens, Mireille M.A.E./ Hydrophobic-interaction-induced stiffening of α -synuclein fibril networks. In: Physical Review Letters. 2018 ; Vol. 120, Nr. 20.
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abstract = "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.",
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Semerdzhiev, SA, Lindhoud, S, Stefanovic, A, Subramaniam, V, van der Schoot, P & Claessens, MMAE 2018, 'Hydrophobic-interaction-induced stiffening of α -synuclein fibril networks' Physical Review Letters, vol 120, nr. 20, 208102. DOI: 10.1103/PhysRevLett.120.208102

Hydrophobic-interaction-induced stiffening of α -synuclein fibril networks. / Semerdzhiev, Slav A.; Lindhoud, Saskia; Stefanovic, Anja; Subramaniam, Vinod; van der Schoot, Paul; Claessens, Mireille M.A.E.

In: Physical Review Letters, Vol. 120, Nr. 20, 208102, 17.05.2018.

Onderzoeksoutput: Bijdrage aan tijdschriftTijdschriftartikel

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Semerdzhiev SA, Lindhoud S, Stefanovic A, Subramaniam V, van der Schoot P, Claessens MMAE. Hydrophobic-interaction-induced stiffening of α -synuclein fibril networks. Physical Review Letters. 2018 mei 17;120(20). 208102. Beschikbaar vanaf, DOI: 10.1103/PhysRevLett.120.208102