Universality in the morphology and mechanics of coarsening amyloid fibril networks

Above a critical concentration a wide variety of peptides and proteins self-assemble into amyloid fibrils which entangle to form percolating networks called hydrogels. Such hydrogels have important applications as biomaterials and in nanotechnology, but their applicability often depends on their mec...

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Bibliographic Details
Published in:arXiv.org 2014-09
Main Authors: Rizzi, Leandro G, Head, David A, Auer, Stefan
Format: Article
Language:English
Subjects:
Biomedical materials
Coarsening
Computer simulation
Hydrogels
Interaction parameters
Mechanical properties
Molecular structure
Morphology
Nanotechnology
Networks
Peptides
Percolation
Proteins
Scaling
Shear modulus
Time dependence
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Summary:Above a critical concentration a wide variety of peptides and proteins self-assemble into amyloid fibrils which entangle to form percolating networks called hydrogels. Such hydrogels have important applications as biomaterials and in nanotechnology, but their applicability often depends on their mechanical properties for which we currently have no predictive capability. Here we use a peptide model to simulate the formation of amyloid fibril networks, and couple these to elastic network theory to determine their mechanical properties. The simulations reveal that the time-dependence of morphological quantities characterizing the network length scales can be collapsed onto master curves by using a time scaling function that depends on the interaction parameter between the peptides. The same scaling function is used to unveil a universal, non-monotonic dependence of the shear modulus with time. The obtained insight into the structure-function relationship between the peptide building blocks, network morphology and network mechanical properties can aid experimentalists to design amyloid fibril networks with tailored mechanical properties.
ISSN:2331-8422
DOI:10.48550/arxiv.1409.6876