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二合一蜘蛛丝蛋白在全水纺丝纤维中具有综合机械性能。

Two-in-One Spider Silk Protein with Combined Mechanical Features in All-Aqueous Spun Fibers.

机构信息

Lehrstuhl Biomaterialien, Universität Bayreuth, Prof.-Rüdiger-Bormann-Str. 1, 95447 Bayreuth, Germany.

Bayreuther Zentrum für Kolloide und Grenzflächen (BZKG), Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, Germany.

出版信息

Biomacromolecules. 2023 Apr 10;24(4):1744-1750. doi: 10.1021/acs.biomac.2c01500. Epub 2023 Mar 13.

DOI:10.1021/acs.biomac.2c01500
PMID:36913547
Abstract

Major ampullate (MA) spider silk reveals outstanding mechanical properties in terms of a unique combination of high tensile strength and extensibility, unmatched by most other known native or synthetic fiber materials. MA silk contains at least two spider silk proteins (spidroins), and here, a novel two-in-one (TIO) spidroin was engineered, resembling amino acid sequences of such two of the European garden spider. The combination of mechanical and chemical features of both underlying proteins facilitated the hierarchical self-assembly into β-sheet-rich superstructures. Due to the presence of native terminal dimerization domains, highly concentrated aqueous spinning dopes could be prepared from recombinant TIO spidroins. Subsequently, fibers were spun in a biomimetic, aqueous wet-spinning process, yielding mechanical properties at least twice as high as fibers spun from individual spidroins or blends. The presented processing route holds great potential for future applications using ecological green high-performance fibers.

摘要

大型壶腹腺(MA)蛛丝在高强度和可拉伸性的独特组合方面表现出出色的机械性能,这是大多数其他已知的天然或合成纤维材料所无法比拟的。MA 丝至少含有两种蛛丝蛋白(丝氨酸蛋白),在此,设计了一种新型的双合一(TIO)丝氨酸蛋白,类似于两种欧洲花园蜘蛛的氨基酸序列。两种基础蛋白的机械和化学特性的结合促进了β-折叠丰富的超结构的分级自组装。由于存在天然的末端二聚化结构域,可以从重组 TIO 丝氨酸蛋白中制备高浓度的纺丝用原丝溶液。随后,采用仿生的、水基湿法纺丝工艺将纤维纺出,所得到的纤维的机械性能至少比由单个丝氨酸蛋白或混合物纺出的纤维高二倍。所提出的加工路线为使用生态绿色高性能纤维的未来应用提供了巨大的潜力。

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