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复性丝素蛋白凝胶的流变学:极端力学的典范

Rheology of reconstituted silk fibroin protein gels: the epitome of extreme mechanics.

作者信息

Tabatabai A Pasha, Kaplan David L, Blair Daniel L

机构信息

Georgetown University, Department of Physics, The Institute for Soft Matter Synthesis and Metrology, Washington, DC 20057, USA.

出版信息

Soft Matter. 2015 Jan 28;11(4):756-61. doi: 10.1039/c4sm02079k. Epub 2014 Dec 9.

Abstract

In nature, silk fibroin proteins assemble into hierarchical structures with dramatic mechanical properties. With the hope of creating new classes of on demand silk-based biomaterials, Bombyx mori silk is reconstituted back into stable aqueous solutions that can be reassembled into functionalized materials; one strategy for reassembly is electrogelation. Electrogels (e-gels) are particularly versatile and can be produced using electrolysis with small DC electric fields. We characterize the linear and nonlinear rheological behavior of e-gels to provide fundamental insights into these distinct protein-based materials. We observe that e-gels form robust biopolymer networks that exhibit distinctive strain hardening and are recoverable from strains as large as γ=27, i.e. 2700%. We propose a simple microscopic model that is consistent with local restructuring of single proteins within the e-gel network.

摘要

在自然界中,丝素蛋白会组装成具有显著机械性能的分级结构。怀着创造新型按需定制的丝基生物材料的希望,家蚕丝被重新制成稳定的水溶液,这些水溶液可重新组装成功能化材料;重新组装的一种策略是电凝胶化。电凝胶(e-凝胶)特别通用,可以通过小直流电场的电解来制备。我们表征了e-凝胶的线性和非线性流变行为,以深入了解这些独特的基于蛋白质的材料。我们观察到e-凝胶形成了强大的生物聚合物网络,这些网络表现出独特的应变硬化,并且可以从高达γ=27(即2700%)的应变中恢复。我们提出了一个简单的微观模型,该模型与e-凝胶网络内单个蛋白质的局部重组相一致。

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