Aufderhorst-Roberts, A, Cussons, S, Brockwell, DJ orcid.org/0000-0002-0802-5937 et al. (1 more author) (2023) Diversity of viscoelastic properties of an engineered muscle-inspired protein hydrogel. Soft Matter, 19 (17). pp. 3167-3178. ISSN 1744-683X
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.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © The Royal Society of Chemistry 2023. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. |
Dates: |
|
Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Physics and Astronomy (Leeds) > Molecular & Nanoscale Physics |
Depositing User: | Symplectic Publications |
Date Deposited: | 23 May 2023 14:12 |
Last Modified: | 23 May 2023 14:26 |
Status: | Published |
Publisher: | Royal Society of Chemistry |
Identification Number: | 10.1039/d2sm01225a |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:199460 |