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新型高溶解性嵌合重组蜘蛛丝蛋白,产量高。

Novel Highly Soluble Chimeric Recombinant Spidroins with High Yield.

机构信息

Institute of Biological Sciences and Biotechnology, Donghua University, Shanghai 201620, China.

出版信息

Int J Mol Sci. 2020 Sep 20;21(18):6905. doi: 10.3390/ijms21186905.

Abstract

Spider silk has been a hotspot in the study of biomaterials for more than two decades due to its outstanding mechanical properties. Given that spiders cannot be farmed, and their low silk productivity, many attempts have been made to produce recombinant spidroins as an alternative. Herein, we present novel chimeric recombinant spidroins composed of 1 to 4 repetitive units of aciniform spidroin (AcSp) flanked by the nonrepetitive N- and C-terminal domains of the minor ampullate spidroin (MiSp), all from The spidroins were expressed in the form of inclusion body in with high yield. Remarkably, the aqueous solubility of the four spidroins ranged from 13.4% to over 50% (). The four spidroins could self-assemble into silk-like fibers by hand-drawing. The secondary structures of these proteins, determined by circular dichroism spectrum (CD) and Fourier transform infrared spectrum (FTIR), indicated a prominent transformation from -helix to -sheet after fiber formation. The mechanical properties of the hand-drawn fibers showed a positive correlation with the spidroin molecular weight. In summary, this study describes promising biomaterials for further study and wide application.

摘要

蜘蛛丝因其出色的机械性能而成为生物材料研究的热点已有二十多年。由于无法养殖蜘蛛,且其丝产量低,因此人们尝试了许多方法来生产重组蜘蛛丝蛋白作为替代品。在此,我们介绍了由 1 到 4 个重复单元的栉状丝蛋白(AcSp)组成的新型嵌合重组蜘蛛丝,两端分别是非重复的 N 端和小蛛丝腺丝蛋白(MiSp)的 C 端,均来自 这些丝蛋白以包涵体的形式在 中大量表达。值得注意的是,这四种丝蛋白的水溶度范围为 13.4%到 50%以上()。这四种丝蛋白可以通过手工拉伸自组装成类似丝的纤维。通过圆二色光谱(CD)和傅里叶变换红外光谱(FTIR)确定的这些蛋白质的二级结构表明,在纤维形成后,-螺旋结构明显转变为 -折叠结构。手工拉伸纤维的力学性能与丝蛋白的分子量呈正相关。总之,这项研究为进一步研究和广泛应用提供了有前景的生物材料。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2e30/7554824/5334f7130d5b/ijms-21-06905-g001.jpg

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