Production and Properties of Triple Chimeric Spidroins,Biomacromolecules

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Production and Properties of Triple Chimeric Spidroins
Biomacromolecules ( IF 5.5 ) Pub Date : 2018-04-18 00:00:00 , DOI: 10.1021/acs.biomac.8b00402
Yizhong Zhou ₁ , Anna Rising _{2,

3} , Jan Johansson ₃ , Qing Meng ₁

Affiliation

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, NTW_1–4CT 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.

中文翻译：

三重嵌合螺旋蛋白的生产及性质

所有蜘蛛丝蛋白（spidroins）均由N端和C端结构域（NT和CT）组成，它们分别调节丝的溶解性和装配性以及中央重复区域，从而赋予纤维机械性能。在七种蜘蛛丝中，,形丝具有最高的韧性。在这里，我们将来自主要和次要壶腹螺旋体（MaSps和MiSps）的NT和CT域分别融合到来自另一种类型的蜘蛛状螺旋体（aciniform spidroin 1（AcSp1））的1-4个重复域（W）中。尽管这三个域起源于远距离相关的spidroin类型，但它们在嵌合spidroin中保持各自的特性。此外，所有的嵌合体spidroins都可以通过手工拉伸形成丝状纤维。与仅从W域以相同方式制造的光纤相反，NTW _1-4CT纤维显示出优异的机械性能。我们的结果表明，可以设计具有NT，CT和重复结构域的嵌合蜘蛛丝蛋白，以形成具有各种机械性能的纤维。

更新日期：2018-04-18

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