Universality in the morphology and mechanics of coarsening amyloid fibril networks

Abstract

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.

arXiv commentArticle (6 pages, 4 figures) + Supplementary Information (6 pages, 6 figures)

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Cited by in corpus (6)

• Amyloid Fibril Solubility
• Microrheological approach for the viscoelastic response of gels
• Importance of non-affine viscoelastic response in disordered fibre networks
• Shape-free theory for the self-assembly kinetics in macromolecular systems
• On the relationship between the plateau modulus and the threshold frequency in peptide gels
• Microrheology of semiflexible filament solutions based on relaxation simulations