Elasticity in Physically Cross-Linked Amyloid Fibril Networks

Yiping Cao, Sreenath Bolisetty, Jozef Adamcik, and Raffaele Mezzenga
Phys. Rev. Lett. 120, 158103 – Published 13 April 2018
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Abstract

We provide a constitutive model of semiflexible and rigid amyloid fibril networks by combining the affine thermal model of network elasticity with the Derjaguin-Landau-Vervey-Overbeek (DLVO) theory of electrostatically charged colloids. When compared to rheological experiments on β-lactoglobulin and lysozyme amyloid networks, this approach provides the correct scaling of elasticity versus both concentration (Gc2.2 and Gc2.5 for semiflexible and rigid fibrils, respectively) and ionic strength (GI4.4 and GI3.8 for β-lactoglobulin and lysozyme, independent from fibril flexibility). The pivotal role played by the screening salt is to reduce the electrostatic barrier among amyloid fibrils, converting labile physical entanglements into long-lived cross-links. This gives a power-law behavior of G with I having exponents significantly larger than in other semiflexible polymer networks (e.g., actin) and carrying DLVO traits specific to the individual amyloid fibrils.

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  • Received 5 October 2017
  • Revised 2 February 2018

DOI:https://doi.org/10.1103/PhysRevLett.120.158103

© 2018 American Physical Society

Physics Subject Headings (PhySH)

Polymers & Soft MatterCondensed Matter, Materials & Applied Physics

Authors & Affiliations

Yiping Cao1, Sreenath Bolisetty1, Jozef Adamcik1, and Raffaele Mezzenga1,2,*

  • 1Department of Health Sciences and Technology, ETH Zurich, Schmelzbergstrasse 9, Zurich 8092, Switzerland
  • 2Department of Materials, ETH Zurich, Wolfgang-Pauli-Strasse 10, Zurich 8093, Switzerland

  • *raffaele.mezzenga@hest.ethz.ch

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Issue

Vol. 120, Iss. 15 — 13 April 2018

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