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.Comment: 13 pages, 6 figure

Claessens, Mireille M. A. E.

Lindhoud, Saskia

Semerdzhiev, Slav A.

Stefanovic, Anja

Subramaniam, Vinod

van der Schoot, Paul

English

arXiv

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

Claessens, Mireille M.A.E.

NARCIS 

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

Van Der Schoot, Paul

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

Sub Algemeen Theoretical Physics

Theoretical Physics

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.</p

VU Research Portal

Slav A. Semerdzhiev

Saskia Lindhoud

Anja Stefanovic

Vinod Subramaniam

Paul van der Schoot

Mireille M. A. E. Claessens

Crossref

Physical Review Letters

Hydrophobic-Interaction-Induced Stiffening of 
<mml:math xmlns:mml="http://www.w3.org/1998/Math/MathML" display="inline"><mml:mi>α</mml:mi></mml:math>
-Synuclein Fibril Networks

\u3cp\u3eIn 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.\u3c/p\u3

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

Abstract

Similar works

Full text

Available Versions

NARCIS

NARCIS

NARCIS

VU Research Portal

Crossref

Repository TU/e

NARCIS