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

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 I27(5), using a multimodal rheology approach. Across multiple protocols, the hydrogels consistently exhibit power-law viscoelasticity in the linear viscoelastic regime with an exponent beta = 0.03, suggesting a dense fractal meso-structure, with predicted fractal dimension d(f) = 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 beta, d(f) 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.

Automated summary

Folded protein hydrogels, inspired by muscle protein titin and engineered to polyprotein I27(5), exhibit diverse viscoelastic properties originating from both nanoscale and mesoscopic scale origins. This study highlights the potential for engineering novel biomaterials with tunable mechanical properties.