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蛛丝蛋白非结晶区不同基序插入RADA16-Ⅰ,短肽分别为R1(n-RADARADAGGASRADARADA-c)和R2(n-RADARADAGPGGYRADARADA-c)。采用傅立叶红外光谱(FTIR)、原子力显微镜(AFM)和透射电子显微镜(TEM)技术研究氨基酸序列和组装时间对短肽的二级结构和自组装成的纳米结构的影响。结果表明,随着时间的延长,R1和R2形成的β-折叠片含量升高,纤维变长变宽。R1形成数量少但长达几十微米的纤维,R2形成长约一微米但数量多的纤维。通过改变氨基酸序列,控制组装时间可以达到控制自组装形成的纳米结构的目的。
RADA16-Ⅰ was inserted into different motifs of non-crystallized spidroin, and the short peptides were n-RADARADAGGASRADARADA-c and n-RADARADAGPGGYRADARADA-c, respectively. The effects of amino acid sequence and assembly time on the secondary structure of short peptides and the self-assembled nanostructures were investigated by Fourier transform infrared spectroscopy (FTIR), atomic force microscopy (AFM) and transmission electron microscopy (TEM). The results showed that with the extension of time, the content of β-sheet formed by R1 and R2 increased, and the fiber became longer and longer. R1 forms a small number of fibers up to several tens of micrometers, and R2 forms a large number of fibers about one micrometer in length. By changing the amino acid sequence and controlling the assembly time, the purpose of controlling the nanostructures formed by self-assembly can be achieved.