Issue 17, 2023

Diversity of viscoelastic properties of an engineered muscle-inspired protein hydrogel

Abstract

Folded protein hydrogels are prime candidates as tuneable biomaterials but it is unclear to what extent their mechanical properties have mesoscopic, as opposed to molecular origins. To address this, we probe hydrogels inspired by the muscle protein titin and engineered to the polyprotein I275, using a multimodal rheology approach. Across multiple protocols, the hydrogels consistently exhibit power-law viscoelasticity in the linear viscoelastic regime with an exponent β = 0.03, suggesting a dense fractal meso-structure, with predicted fractal dimension df = 2.48. In the nonlinear viscoelastic regime, the hydrogel undergoes stiffening and energy dissipation, indicating simultaneous alignment and unfolding of the folded proteins on the nanoscale. Remarkably, this behaviour is highly reversible, as the value of β, df and the viscoelastic moduli return to their equilibrium value, even after multiple cycles of deformation. This highlights a previously unrevealed diversity of viscoelastic properties that originate on both at the nanoscale and the mesoscopic scale, providing powerful opportunities for engineering novel biomaterials.

Graphical abstract: Diversity of viscoelastic properties of an engineered muscle-inspired protein hydrogel

Supplementary files

Article information

Article type
Paper
Submitted
10 Sep 2022
Accepted
24 Mar 2023
First published
28 Mar 2023
This article is Open Access
Creative Commons BY license

Soft Matter, 2023,19, 3167-3178

Diversity of viscoelastic properties of an engineered muscle-inspired protein hydrogel

A. Aufderhorst-Roberts, S. Cussons, D. J. Brockwell and L. Dougan, Soft Matter, 2023, 19, 3167 DOI: 10.1039/D2SM01225A

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