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Investigation of Rheological Properties and Conformation of Silk Fibroin in the Solution of AmimCI

机译:AmimCI溶液中丝素蛋白的流变性质和构象研究

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摘要

The conformation and eventual morphology of silk fibroin (SF) chains are crucial for the mechanical properties of SF materials, and are strongly related to the solvation step as a key stage in their processing conditions. In this work, a novel SF/AmimCl (l-allyl-3-methylimidazolium chloride) solution with unique properties is reported and compared with conventional regenerated SF aqueous solutions, based on an investigation of its rheological properties. The steady shearing behavior suggested that AmimCI is a good solvent for SF molecules, and shear thinning of semidiluted SF/AmimCl solution at high shearrates showed behavior similar to that in native spinning, which is due to the rearrangement and orientation of SF molecular chains. Fitting of experimental dynamic viscoelastic data to the Rouse model provided an effective method to estimate the molecular weight of SF. We believe that this work not only provides a better understanding of the relationship between properties of silk protein and aggregation states of their molecular chains, but also provides tools to fabricate high-performance SF-based materials.
机译:丝素蛋白(SF)链的构象和最终形态对于SF材料的机械性能至关重要,并且与溶剂化步骤密切相关,而溶剂化步骤是其加工条件中的关键阶段。在这项工作中,基于流变学特性的研究,报道了一种具有独特性能的新型SF / AmimCl(1-烯丙基-3-甲基咪唑鎓氯化物)溶液,并将其与常规再生SF水溶液进行了比较。稳定的剪切行为表明AmimCI是SF分子的良好溶剂,半稀释SF / AmimCl溶液在高剪切速率下的剪切稀化显示出与天然纺丝相似的行为,这是由于SF分子链的重排和取向所致。将实验动态粘弹性数据拟合到Rouse模型提供了一种估算SF分子量的有效方法。我们认为,这项工作不仅可以更好地理解丝蛋白的性质与其分子链的聚集状态之间的关系,而且还可以提供制造基于SF的高性能材料的工具。

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