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 Araneus ventricosus. The spidroins were expressed in the form of inclusion body in E. coli with high yield. Remarkably, the aqueous solubility of the four spidroins ranged from 13.4% to over 50% (m/v). 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 α-helix to β-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.
Highlights
Spider silks are the toughest known natural silk fibers, and have received much attention in the field of biomaterials [1,2]
The Nand C-terminal domains are more conserved across different spidroins [7], and both play a critical role in spidroin storage in the gland and the initiation of the fiber assembly process [8], while the central repetitive domain is less conserved and tailored for the individual mechanical functions of the different silk types [9,10]
We produced a series of novel recombinant spidroins based on 1 to 4 repetitive units of aciniform spidroin (AcSp), N-terminal domain (NT), and C-terminal domain (CT) of minor ampullate spidroin (MiSp) from Araneus ventricosus
Summary
Spider silks are the toughest known natural silk fibers, and have received much attention in the field of biomaterials [1,2]. The Nand C-terminal domains are more conserved across different spidroins [7], and both play a critical role in spidroin storage in the gland and the initiation of the fiber assembly process [8], while the central repetitive domain is less conserved and tailored for the individual mechanical functions of the different silk types [9,10] It consists of modular units with different lengths in different spidroins; the modular units can repeat up to approximately 100 times within the core domain [10,11,12]
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