Abstract：Abstract: Spiders can produce seven different types of silks or glues with different mechanical properties. Among them, flagelliform silk has the best elasticity, and dragline silk has the highest strength. Herein, one repetitive module of flagelliform spidroin (Flag) and one repetitive module of major ampullate spidroin (MaSp1) from Araneus ventricosus were fused. The chimeric spidroin FlagR-MaSp1R expressed by E. coli can be self-assembled to silk-like fibers by shear force. Further circular dichroism (CD) spectrum analysis showed that the secondary structure of FlagR-MaSp1R protein in solution was dominated by α-helix at pH 7.0. However, in the process of fiber-forming, the secondary structure of FlagR-MaSp1R was changed from α-helix to β-sheet as indicated by Fourier transform infrared spectroscopy (FTIR). Observation under scanning electron microscope (SEM) revealed that the chimeric silk fiber has smooth surface, and its diameter was 1~2 μm, which was similar to that of natural silks. The results provide theoretical basis and method support for the preparation of chimeric spider silk fibers with specific functions.
引用本文:
田露阳, 孟 清, 林 瑛. 嵌合蛛丝蛋白Flag-MaSp1重复模块的表达及二级结构分析[J]. 生命科学研究, 2020, 24(5): 396-403. TIAN Lu-yang, MENG Qing, LIN Ying. Expression and Secondary Structure Analysis of Chimeric Spidroin from Flag-MaSp1 Repetitive Modules. Life Science Research, 2020, 24(5): 396-403.
