Super Bacteria: A New Hope of Manufacturing Spider Silk in an Efficient Way

The important properties of spider dragline silk and other protein polymers will find many applications. We have demonstrated the production of spider silk, which has many important properties, are produced from the bacteria including Escherichia coli. The productions of high molecular weight spider drag line encoded by synthetic genes. Silk protein can be efficiently produced by the microbial system has become an advantageous method like quick secretion and simple product recovery has become an efficient method .From the observation of various experiments done by several scientists has shown silk made in laboratory. The study of RIKEN centre for sustainable resource science has shown that spider silk can be produce huge amount. Observation shown that joining of the fragments by split intein sequence which then cut itself to yield full name protein .Spun into fibers make the microbial spider silk tough , stretchable and stronger. Better modification of bioengineering can increase the amount of production.

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Artificial spider silk is smart like natural one: having humidity-sensitive shape memory with superior recovery stress

Materials Chemistry Frontiers ◽

10.1039/c9qm00261h ◽

2019 ◽

Vol 3 (11) ◽

pp. 2472-2482 ◽

Cited By ~ 2

Author(s):

Harun Venkatesan ◽

Jianming Chen ◽

Haiyang Liu ◽

Yoonjung Kim ◽

Sungsoo Na ◽

...

Keyword(s):

Shape Memory ◽

Spider Silk ◽

Recovery Stress ◽

Dragline Silk ◽

Spider Dragline Silk ◽

Shape Memory Behaviour

Inspired by supercontraction, the recombinant spider dragline silk displayed humidity-responsive shape memory behaviour with impressive recovery stress.

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Hyper-production of large proteins of spider dragline silk MaSp2 by Escherichia coli via synthetic biology approach

Process Biochemistry ◽

10.1016/j.procbio.2016.01.006 ◽

2016 ◽

Vol 51 (4) ◽

pp. 484-490 ◽

Cited By ~ 14

Author(s):

Yan-Xiang Yang ◽

Zhi-Gang Qian ◽

Jian-Jiang Zhong ◽

Xiao-Xia Xia

Keyword(s):

Escherichia Coli ◽

Synthetic Biology ◽

Dragline Silk ◽

Large Proteins ◽

Spider Dragline Silk ◽

Synthetic Biology Approach

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Tensegrity Modelling and the High Toughness of Spider Dragline Silk

Nanomaterials ◽

10.3390/nano10081510 ◽

2020 ◽

Vol 10 (8) ◽

pp. 1510

Author(s):

Fernando Fraternali ◽

Nicola Stehling ◽

Ada Amendola ◽

Bryan Andres Tiban Anrango ◽

Chris Holland ◽

...

Keyword(s):

Spider Silk ◽

Low Voltage ◽

Microstructural Characterization ◽

Hierarchical Organization ◽

Air Plasma ◽

Poisson Effect ◽

Dragline Silk ◽

Spider Dragline Silk ◽

A Chain ◽

Spider Silks

This work establishes a tensegrity model of spider dragline silk. Tensegrity systems are ubiquitous in nature, being able to capture the mechanics of biological shapes through simple and effective modes of deformation via extension and contraction. Guided by quantitative microstructural characterization via air plasma etching and low voltage scanning electron microscopy, we report that this model is able to capture experimentally observed phenomena such as the Poisson effect, tensile stress-strain response, and fibre toughness. This is achieved by accounting for spider silks’ hierarchical organization into microfibrils with radially variable properties. Each fibril is described as a chain of polypeptide tensegrity units formed by crystalline granules operating under compression, which are connected to each other by amorphous links acting under tension. Our results demonstrate, for the first time, that a radial variability in the ductility of tensegrity chains is responsible for high fibre toughness, a defining and desirable feature of spider silk. Based on this model, a discussion about the use of graded tensegrity structures for the optimal design of next-generation biomimetic fibres is presented.

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Nanostructure and molecular mechanics of spider dragline silk protein assemblies

Journal of The Royal Society Interface ◽

10.1098/rsif.2010.0149 ◽

2010 ◽

Vol 7 (53) ◽

pp. 1709-1721 ◽

Cited By ~ 156

Author(s):

Sinan Keten ◽

Markus J. Buehler

Keyword(s):

Secondary Structure ◽

Spider Silk ◽

Mechanical Performance ◽

Experimental Studies ◽

Silk Protein ◽

Nephila Clavipes ◽

Protein Assemblies ◽

Dragline Silk ◽

Spider Dragline Silk ◽

Secondary Structure Content

Spider silk is a self-assembling biopolymer that outperforms most known materials in terms of its mechanical performance, despite its underlying weak chemical bonding based on H-bonds. While experimental studies have shown that the molecular structure of silk proteins has a direct influence on the stiffness, toughness and failure strength of silk, no molecular-level analysis of the nanostructure and associated mechanical properties of silk assemblies have been reported. Here, we report atomic-level structures of MaSp1 and MaSp2 proteins from the Nephila clavipes spider dragline silk sequence, obtained using replica exchange molecular dynamics, and subject these structures to mechanical loading for a detailed nanomechanical analysis. The structural analysis reveals that poly-alanine regions in silk predominantly form distinct and orderly beta-sheet crystal domains, while disorderly regions are formed by glycine-rich repeats that consist of 3 1 -helix type structures and beta-turns. Our structural predictions are validated against experimental data based on dihedral angle pair calculations presented in Ramachandran plots, alpha-carbon atomic distances, as well as secondary structure content. Mechanical shearing simulations on selected structures illustrate that the nanoscale behaviour of silk protein assemblies is controlled by the distinctly different secondary structure content and hydrogen bonding in the crystalline and semi-amorphous regions. Both structural and mechanical characterization results show excellent agreement with available experimental evidence. Our findings set the stage for extensive atomistic investigations of silk, which may contribute towards an improved understanding of the source of the strength and toughness of this biological superfibre.

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Cloning and Expression of Spider Dragline Silk Protein Gene in Escherichia coli and Eukaryotic Cells

Molecular Entomology ◽

10.5376/me.2011.02.0001 ◽

2011 ◽

Author(s):

Li Wenli

Keyword(s):

Escherichia Coli ◽

Protein Gene ◽

Silk Protein ◽

Cloning And Expression ◽

Eukaryotic Cells ◽

Dragline Silk ◽

Spider Dragline Silk

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Scalable Spider Silk Inspired Materials with High Extensibility and Super Toughness

Key Engineering Materials ◽

10.4028/www.scientific.net/kem.893.31 ◽

2021 ◽

Vol 893 ◽

pp. 31-35

Author(s):

Jin Lian Hu ◽

Yuan Zhang Jiang ◽

Lin Gu

Keyword(s):

Chemical Synthesis ◽

Spider Silk ◽

Helical Structure ◽

Silk Proteins ◽

Dragline Silk ◽

Spider Dragline Silk ◽

Argiope Trifasciata ◽

Chemical Synthesis Route ◽

Β Sheet ◽

Huge Challenge

Spiders silks have extraordinary strength and toughness simultaneously, thus has become dreamed materials by scientists and industries. Although there have been tremendous attempts to prepare fibers from genetically manufacture spider silk proteins, however, it has been still a huge challenge because of tedious procedure and high cost. Here, a facile spider-silk-mimicking strategy is reported for preparing highly scratchable polymers and supertough fibers from chemical synthesis route. Polymer films with high extensibility (>1200%) and supertough fibers (~387 MJ m-3) are achieved by introducing polypeptides with β-sheet and α-helical structure in polyureathane/urea polymers. Notabley,the toughness of the fiber is more than twice the reported value of a normal spider dragline silk, and comparable with the toughest spider silk, aciniform silk of Argiope trifasciata.

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