1P034 Molecular and mechanical properties of spider silk(Proteins-functions,Poster Presentations)

The properties of native spider silk vary within and across species due to the presence of different genes containing conserved repetitive core domains encoding a variety of silk proteins. Previous studies seeking to understand the function and material properties of these domains focused primarily on the analysis of dragline silk proteins, MaSp1 and MaSp2. Our work seeks to broaden the mechanical properties of silk-based biomaterials by establishing two libraries containing genes from the repetitive core region of the native Latrodectus hesperus silk genome (Library A: genes masp1, masp2, tusp1, acsp1; Library B: genes acsp1, pysp1, misp1, flag). The expressed and purified proteins were analyzed through Fourier Transform Infrared Spectrometry (FTIR). Some of these new proteins revealed a higher portion of β-sheet content in recombinant proteins produced from gene constructs containing a combination of masp1/masp2 and acsp1/tusp1 genes than recombinant proteins which consisted solely of dragline silk genes (Library A). A higher portion of β-turn and random coil content was identified in recombinant proteins from pysp1 and flag genes (Library B). Mechanical characterization of selected proteins purified from Library A and Library B formed into films was assessed by Atomic Force Microscopy (AFM) and suggested Library A recombinant proteins had higher elastic moduli when compared to Library B recombinant proteins. Both libraries had higher elastic moduli when compared to native spider silk proteins. The preliminary approach demonstrated here suggests that repetitive core regions of the aforementioned genes can be used as building blocks for new silk-based biomaterials with varying mechanical properties.

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Hypotheses that correlate the sequence, structure, and mechanical properties of spider silk proteins

International Journal of Biological Macromolecules ◽

10.1016/s0141-8130(98)00089-0 ◽

1999 ◽

Vol 24 (2-3) ◽

pp. 271-275 ◽

Cited By ~ 380

Author(s):

Cheryl Y. Hayashi ◽

Nichola H. Shipley ◽

Randolph V. Lewis

Keyword(s):

Mechanical Properties ◽

Spider Silk ◽

Sequence Structure ◽

Silk Proteins

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“Biosteel”: an exciting product from nature that is superior to many manmade alternatives

Reviews in Chemical Engineering ◽

10.1515/revce-2014-0055 ◽

2015 ◽

Vol 31 (5) ◽

Author(s):

Soumyadip Majumder ◽

Mahadev D. Kaulaskar ◽

Sudarsan Neogi

Keyword(s):

Mechanical Properties ◽

Cell Culture ◽

Production Process ◽

Spider Silk ◽

Review Paper ◽

Silk Proteins ◽

Cell Culture Techniques ◽

Culture Techniques ◽

Synthetic Fibers

AbstractBiotechnology continues to offer routes for many exciting and unique products. Researchers genetically altered goats with a spider gene. These goats produce milk that contains a protein that can be extracted to produce biosteel fibers for use in bulletproof vests. It is referred to as “biosteel” to highlight its strength comparable to steel. This review paper describes the important aspects of produced dragline spider silk proteins via cell culture techniques using silk genes derived from two species of weaving spiders. These fibers were tested for a number of mechanical properties and compared to natural spider silk. In effect, fibers of biosteel were able to absorb similar amounts of energy as natural spider silk by stretching further. As opposed to most other synthetic fibers, biosteel is ecofriendly both in terms of its composition and production process.

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Preparation and mechanical properties of layers made of recombinant spider silk proteins and silk from silk worm

Applied Physics A ◽

10.1007/s00339-005-3432-9 ◽

2005 ◽

Vol 82 (2) ◽

pp. 253-260 ◽

Cited By ~ 41

Author(s):

F. Junghans ◽

M. Morawietz ◽

U. Conrad ◽

T. Scheibel ◽

A. Heilmann ◽

...

Keyword(s):

Mechanical Properties ◽

Spider Silk ◽

Silk Proteins ◽

Silk Worm

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Mechanical Properties of Spider Silk for Use As a Biomaterial: Molecular Dynamics Investigations

Volume 3: Advanced Materials: Design, Processing, Characterization, and Applications ◽

10.1115/imece2020-23951 ◽

2020 ◽

Author(s):

Atul Rawal ◽

Kristen L. Rhinehardt ◽

Ram V. Mohan

Keyword(s):

Mechanical Properties ◽

Molecular Dynamics ◽

Spider Silk ◽

Complete Separation ◽

Silk Protein ◽

Silk Proteins ◽

Silk Fibers ◽

Spider Silk Protein ◽

Β Chain ◽

Smd Simulations

Abstract Even though silkworm are the most dominant type of silk fibers used for commercial applications, spider silk has a definitive role in biomedical applications due to its biocompatibility and excellent mechanical properties as biomaterials. In recent years, recombinant production of the silk proteins at a larger scale has found new interest. Spider silk composites with a combination of a variety of other biomaterials have also been used to improve properties such as bio-compatibility, mechanical strength and controlled degradation. [1] A major constituent of spider silk fibers, are spidroin proteins. These are made up of repetitive segments flanked by conserved non-repetitive domains. The fiber proteins consist of a light chain and a heavy chain that are connected via a single disulfide bond. [2] Present paper employed steered molecular dynamics (SMD) as the principal method of investigating the mechanical properties of these nanoscale spider silk protein 3LR2, with a residual count of 134 amino acids. [3]. SMD simulations were performed by pulling on β-chain of the protein in the x-direction, while holding the other fixed. The focus of this paper is to investigate the mechanical properties of the nanoscale spider silk proteins with lengths of about 4.5nm in a folded state, leading to understanding of their feasibility in bio-printing of a composite spider silk biomaterial with a blend of various other biomaterials such as collagen. An in-depth insight into the fraying and tensile deformation and structural properties of the spider silk proteins are of innovative significance for a multitude of biomedical engineering applications. A calculated Gibbs free energy value of 18.59 kCal/mol via umbrella sampling corresponds with a complete separation of a single chain from a spider silk protein in case of fraying. Force needed for complete separation of the chain from the spider silk protein is analyzed, and discussed in this paper. It is found that the protein molecule undergoes a tensile stretch at strain rates of ≅ 11.65. An elastic modulus of 20.136 GPa, calculated via simple SMD simulations by subjecting the silk β-chain to a tensile stretch is also presented.

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Designing of spider silk proteins for hiPSC-based cardiac tissue engineering

Materials Today Bio ◽

10.1016/j.mtbio.2021.100114 ◽

2021 ◽

pp. 100114

Author(s):

Tilman U. Esser ◽

Vanessa T. Trossmann ◽

Sarah Lentz ◽

Felix B. Engel ◽

Thomas Scheibel

Keyword(s):

Tissue Engineering ◽

Spider Silk ◽

Cardiac Tissue ◽

Cardiac Tissue Engineering ◽

Silk Proteins

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Cribellate thread production as model for spider’s spinneret kinematics

Journal of Comparative Physiology A ◽

10.1007/s00359-020-01460-4 ◽

2021 ◽

Author(s):

Margret Weissbach ◽

Marius Neugebauer ◽

Anna-Christin Joel

Keyword(s):

Molecular Structure ◽

Mechanical Properties ◽

Fibre Type ◽

Material Science ◽

Spider Silk ◽

Functional Unit ◽

Material Strength ◽

Spinning Process ◽

Fibre Spinning ◽

House Spider

AbstractSpider silk attracts researchers from the most diverse fields, such as material science or medicine. However, still little is known about silk aside from its molecular structure and material strength. Spiders produce many different silks and even join several silk types to one functional unit. In cribellate spiders, a complex multi-fibre system with up to six different silks affects the adherence to the prey. The assembly of these cribellate capture threads influences the mechanical properties as each fibre type absorbs forces specifically. For the interplay of fibres, spinnerets have to move spatially and come into contact with each other at specific points in time. However, spinneret kinematics are not well described though highly sophisticated movements are performed which are in no way inferior to the movements of other flexible appendages. We describe here the kinematics for the spinnerets involved in the cribellate spinning process of the grey house spider, Badumna longinqua, as an example of spinneret kinematics in general. With this information, we set a basis for understanding spinneret kinematics in other spinning processes of spiders and additionally provide inspiration for biomimetic multiple fibre spinning.

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