Institute of Biological Sciences and Biotechnology , Donghua University , Shanghai 201620 , People's Republic of China.
Department of Anatomy, Physiology and Biochemistry , Swedish University of Agricultural Sciences , Uppsala , Sweden.
Biomacromolecules. 2018 Jul 9;19(7):2825-2833. doi: 10.1021/acs.biomac.8b00402. Epub 2018 May 31.
All spider silk proteins (spidroins) are composed of N- and C-terminal domains (NT and CT) that act as regulators of silk solubility and assembly and a central repetitive region, which confers mechanical properties to the fiber. Among the seven types of spider silks, aciniform silk has the highest toughness. Herein, we fused NT and CT domains from major and minor ampullate spidroins (MaSps and MiSps), respectively, to 1-4 repeat domains (W) from another type of spidroin, aciniform spidroin 1(AcSp1). Although the three domains originate from distantly related spidroin types, they keep their respective characteristics in the chimeric spidroins. Furthermore, all chimeric spidroins could form silk-like fibers by manual-drawing. In contrast to fibers made in the same manner from W domains only, NTWCT fibers show superior mechanical properties. Our results suggest that chimeric spidroins with NT, CT, and repeat domains can be designed to form fibers with various mechanical properties.
所有蜘蛛丝蛋白（丝氨酸）都由 N-和 C-末端结构域（NT 和 CT）组成，这些结构域作为丝溶解性和组装的调节剂，以及中央重复区域，赋予纤维机械性能。在七种类型的蜘蛛丝中，刺丝的韧性最高。在此，我们分别将主要和次要壶腹丝（MaSps 和 MiSps）的 NT 和 CT 结构域融合到来自另一种丝氨酸，刺丝氨酸 1（AcSp1）的 1-4 重复结构域（W）中。尽管这三个结构域源自远缘丝氨酸类型，但它们在嵌合丝氨酸中保留了各自的特征。此外，所有嵌合丝氨酸都可以通过手动拉丝形成类似丝的纤维。与仅由 W 结构域以相同方式制成的纤维相比，NTWCT 纤维表现出更好的机械性能。我们的结果表明，具有 NT、CT 和重复结构域的嵌合丝氨酸可以设计成形成具有各种机械性能的纤维。
