Acta Biomaterialia ( IF 9.4 ) Pub Date : 2020-08-13 , DOI: 10.1016/j.actbio.2020.08.009 Rui Wen 1 , Kangkang Wang 1 , Qing Meng 1
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Spiders spin a range of silks from different glands for distinct functions, and each silk type exhibits distinct material properties. Silk extruded by the aciniform gland is used for prey wrapping and egg case construction and displays high toughness and extensibility. So far, only the aciniform spidroin 1 (AcSp1) gene which was firstly identified as a silk gene in aciniform gland has been obtained. Here we present the gene sequence for the second type of full-length aciniform silk protein, AcSp2. Analysis of the AcSp2 primary sequence reveals relatively conserved terminal regions and a distinct repetitive sequence relative to AcSp1. A fraction of the gene can be expressed in recombinant systems. Secondary structure analysis of the recombinant AcSp2 protein in solution reveals that the protein adopts mainly an α-helical conformation. Artificial spinning of recombinant AcSp2 demonstrates that the spidroins can be spun into fine fibers which display up to 142% extensibility. The silk fibers are dominated by β-sheet and β-turn secondary structures. Moreover, the mechanical data collected from these synthetic fibers revealed that the mechanical properties are partly correlated with the molecular weights. Overall, our studies enrich our knowledge of spidroin gene family members and provide a new insight into creation of high-performance silk fibers for next generation biomaterials.
Statement of Significance
In this study, we presented the second type of aciniform silk protein (AcSp2) gene sequence of orb-weaving spider Araneus ventricosus, expanding the spider silk gene family members. The primary structure revealed the central repetitive sequence of the new spidroin gene is distinctly different from other AcSp1 genes. Characterization of the recombinant minispidroin fibers of AcSp2 revealed the mechanical properties are partly correlate with the molecular weights, and the spidroins can be spun into fine fibers which display up to 142% extensibility. Overall, our studies enrich our knowledge of spidroin gene family members and provide a new insight into creation of high-performance silk fibers for next generation biomaterials.
中文翻译：
第二种aciniform spidroin（AcSp2）的表征为基于spidroin的生物材料的设计提供了新的见识。
蜘蛛会旋转来自不同腺体的一系列丝线，以发挥不同的功能，每种丝线都具有不同的材料特性。腺状腺挤压出的蚕丝被用于猎物包装和蛋盒构造，并具有很高的韧性和延展性。迄今为止，仅获得了最初被鉴定为腺样腺中的丝基因的腺样蜘蛛蛋白1（AcSp1）基因。在这里，我们介绍了第二种全长腺样丝蛋白AcSp2的基因序列。对AcSp2主序列的分析揭示了相对保守的末端区域和相对于AcSp1的独特重复序列。该基因的一部分可以在重组系统中表达。溶液中重组AcSp2蛋白的二级结构分析表明，该蛋白主要采用α-螺旋构象。重组AcSp2的人工纺丝表明，可以将spidroins纺制成细纤维，该细纤维可显示高达142％的可扩展性。丝纤维以β-折叠和β-转二级结构为主。而且，从这些合成纤维收集的机械数据表明，机械性能与分子量部分相关。总体而言，我们的研究丰富了我们对spidroin基因家族成员的了解，并为创建下一代生物材料的高性能丝纤维提供了新的见解。从这些合成纤维收集的机械数据表明，机械性能与分子量部分相关。总体而言，我们的研究丰富了我们对spidroin基因家族成员的了解，并为创建下一代生物材料的高性能丝纤维提供了新的见解。从这些合成纤维收集的机械数据表明，机械性能与分子量部分相关。总体而言，我们的研究丰富了我们对spidroin基因家族成员的了解，并为创建下一代生物材料的高性能丝纤维提供了新的见解。
重要声明
在这项研究中，我们提出了织球蜘蛛Araneus ventricosus的第二种腺样丝蛋白（AcSp2）基因序列，扩展了蜘蛛丝基因家族成员。一级结构揭示了新的spidroin基因的中央重复序列与其他AcSp1基因明显不同。AcSp2的重组小蜘蛛蛋白纤维的表征表明，其机械性能与分子量部分相关，并且可以将蜘蛛蛋白纺丝成细纤维，其显示出高达142％的可扩展性。总体而言，我们的研究丰富了我们对spidroin基因家族成员的了解，并为创建下一代生物材料的高性能丝纤维提供了新的见解。
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