Diversity of viscoelastic properties of an engineered muscle-inspired protein hydrogel.
Diversity of viscoelastic properties of an engineered muscle-inspired protein hydrogel.
复制标题
工程肌肉启发的蛋白质水凝胶的粘弹性特性的多样性。
DOI：
10.1039/d2sm01225a
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发表时间：
2023
期刊：
影响因子：
3.4
通讯作者：
Aufderhorst-Roberts A
中科院分区：
文献类型：
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作者：
Aufderhorst-Roberts A
折叠蛋白质水凝胶是可调节生物材料的主要候选者，但目前尚不清楚其机械性能在多大程度上具有介观性质，而不是分子起源。为了解决这个问题，我们利用多模式流变学方法探索了受肌肉蛋白肌联启发并设计为多蛋白 I275 的水凝胶。在多种方案中，水凝胶始终在线性粘弹性状态下表现出幂律粘弹性，指数 β = 0.03，表明其具有致密的分形细观结构，预测的分形维数 df = 2.48。在非线性粘弹性状态下，水凝胶经历硬化和能量耗散，表明折叠蛋白质在纳米尺度上同时排列和展开。值得注意的是，这种行为是高度可逆的，即使在多次变形循环之后，β、df 和粘弹性模量的值也会恢复到其平衡值。这凸显了先前未揭示的源自纳米尺度和介观尺度的粘弹性特性的多样性，为工程新型生物材料提供了强大的机会。
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.