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Silk i structure formation through silk fibroin self-assembly

机译:通过丝素蛋白自组装形成丝i结构

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摘要

Regenerated silk fibroin films are normally produced by increasing the Silk II structure (β-sheet content). In the present study, silk fibroin films were prepared by controlling the environmental temperature and humidity, resulting in the formation of silk films with a predominant Silk I structure instead of Silk II structure. Wide angle X-ray diffraction indicated that when the relative humidity was 55%, the silk films prepared were mainly composed of Silk I structure, whereas silk films formed on other relative humidity had a higher Silk II structure. Fourier transform infrared analysis (FTIR) results also conformed that the secondary structure of silk fibroin can be controlled by changing the humidity of the films formed process. Thermal analysis results revealed Silk I structure was a stable crystal, and the degradation peak increased to 320°C, indicating a greater thermal stability of these films formed under the 55% relative humidity conditions. Atomic force microscopy (AFM) results depicted silk fibroin in the fresh solution had many nanospheres existing with 20-50 nm diameters and mainly maintained a random coil structure without specific nanostructures. At the same time, it also illustrated the self-assembly process of silk fibroin in the aqueous solution without any human intervention. In addition, this present study also provided additional support for self-assembly mechanism of silk fibroin films formation.
机译:再生的丝素蛋白膜通常是通过增加Silk II结构(β-片层含量)来生产的。在本研究中,通过控制环境温度和湿度来制备丝素蛋白膜,从而形成具有主要Silk I结构而非Silk II结构的丝绸膜。广角X射线衍射表明,当相对湿度为55%时,制备的丝膜主要由Silk I结构组成,而在其他相对湿度下形成的丝膜具有较高的Silk II结构。傅里叶变换红外分析(FTIR)结果也表明,可以通过改变成膜过程的湿度来控制丝素蛋白的二级结构。热分析结果表明Silk I结构是稳定的晶体,降解峰增加到320℃,表明在55%相对湿度条件下形成的这些膜具有更高的热稳定性。原子力显微镜(AFM)结果表明,新鲜溶液中的丝素蛋白具有许多存在的直径为20-50 nm的纳米球,并且主要保持无规卷曲结构而没有特定的纳米结构。同时,它也说明了丝素蛋白在水溶液中的自组装过程,无需任何人工干预。此外,本研究还为丝素蛋白膜形成的自组装机制提供了额外的支持。

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