Lehrstuhl Biomaterialien, Universität Bayreuth, Prof-Rüdiger-Bormann-Str. 1, Bayreuth, 95447, Germany.
Adv Mater. 2021 Mar;33(9):e2006499. doi: 10.1002/adma.202006499. Epub 2021 Jan 26.
Major ampullate (MA) spider silk has fascinating mechanical properties combining strength and elasticity. All known natural MA silks contain at least two or more different spidroins; however, it is unknown why and if there is any interplay in the spinning dope. Here, two different spidroins from Araneus diadematus are co-produced in Escherichia coli to study the possible dimerization and effects thereof on the mechanical properties of fibers. During the production of the two spidroins, a mixture of homo- and heterodimers is formed triggered by the carboxyl-terminal domains. Interestingly, homodimeric species of the individual spidroins self-assemble differently in comparison to heterodimers, and stoichiometric mixtures of homo- and heterodimers yield spidroin networks upon assembly with huge impact on fiber mechanics upon spinning. The obtained results provide the basis for man-made tuning of spinning dopes to yield high-performance fibers.
大型壶腹腺（MA）蛛丝具有迷人的机械性能，兼具强度和弹性。所有已知的天然 MA 丝都至少含有两种或更多不同的丝蛋白；然而，目前尚不清楚为什么以及是否存在纺丝原液中的相互作用。在这里，两种来自大腹园蛛的不同丝蛋白在大肠杆菌中共表达，以研究可能的二聚化及其对纤维机械性能的影响。在两种丝蛋白的生产过程中，由羧基末端结构域触发形成了同源和异源二聚体的混合物。有趣的是，与异源二聚体相比，单个丝蛋白的同源二聚体的自组装方式不同，并且同聚和异聚二聚体的化学计量混合物在组装时形成丝蛋白网络，对纺丝时的纤维力学性能有巨大影响。所得结果为人工调整纺丝原液以获得高性能纤维提供了基础。
