scholarly journals Nephila clavipes Flagelliform Silk-Like GGX Motifs Contribute to Extensibility and Spacer Motifs Contribute to Strength in Synthetic Spider Silk Fibers

2013 ◽  
Vol 14 (6) ◽  
pp. 1751-1760 ◽  
Author(s):  
Sherry L. Adrianos ◽  
Florence Teulé ◽  
Michael B. Hinman ◽  
Justin A. Jones ◽  
Warner S. Weber ◽  
...  
Keyword(s):  
Spider Silk ◽  
Nephila Clavipes ◽  
Silk Fibers

Description of Test Setup and Approach to Measure Thermal Properties of Natural and Synthetic Spider Silks at Cryogenic Temperatures

2013 ◽  
Author(s):  
Troy Munro ◽  
Changhu Xing ◽  
Andrew Marquette ◽  
Heng Ban ◽  
Cameron Copeland ◽  
...  
Keyword(s):  
Thermal Properties ◽  
Conformational Changes ◽  
Spider Silk ◽  
Protein Structures ◽  
Cryogenic Temperatures ◽  
Nephila Clavipes ◽  
Silk Fibers ◽  
Spider Silks ◽  
Better Than ◽  
Natural And Synthetic

Spider silk is well-known for its exceptional mechanical properties, such as strength, elasticity and flexibility. Recently, it has been reported that dragline silk from a Nephila clavipes also has an exceptionally high thermal conductivity, comparable to copper when the fiber is stretched. Synthetic spider silks have been spun from spider silk proteins produced in transgenic sources, and their production process has the optimization potential to have properties similar to or better than the natural spider silk. There is interest to measure the thermal properties of natural and synthetic silk at cryogenic temperatures for use of spider silk fibers as heat conduits in systems where component weight is an issue, such as in spacecraft. This low temperature measurement is also of particular interest because of the conformational changes in protein structures, which affect material properties, that occurs at lower temperatures for some proteins. A measurement system has been designed and is being tested to characterize the thermal properties of natural and synthetic spider silks by means of a transient electrothermal method.

Anisotropic nanomechanical properties of Nephila clavipes dragline silk

2006 ◽  
Vol 21 (8) ◽  
pp. 2035-2044 ◽  
Author(s):  
Donna M. Ebenstein ◽  
Kathryn J. Wahl
Keyword(s):  
Mechanical Properties ◽  
Spider Silk ◽  
Imaging Techniques ◽  
Dynamic Stiffness ◽  
Longitudinal Section ◽  
Mechanical Anisotropy ◽  
Nephila Clavipes ◽  
Silk Fibers ◽  
Reduced Modulus ◽  
Anisotropic Mechanical Properties

Spider silk is a material with unique mechanical properties under tension. In this study, we explore the anisotropic mechanical properties of spider silk using instrumented indentation. Both quasistatic indentation and dynamic stiffness imaging techniques were used to measure the mechanical properties in transverse and longitudinal sections of silk fibers. Quasistatic indentation yielded moduli of 10 ± 2 GPa in transverse sections and moduli of 6.4 ± 0.5 GPa in longitudinal sections, demonstrating mechanical anisotropy in the fiber. This result was supported by dynamic stiffness imaging, which also showed the average reduced modulus measured in the transverse section to be slightly higher than that of the longitudinal section. Stiffness imaging further revealed an oriented microstructure in the fiber, showing microfibrils aligned with the drawing axis of the fiber. No spatial distribution of modulus across the silk sections was observed by either quasistatic or stiffness imaging mechanics.

High‐toughness Spider Silk Fibers Spun from Soluble Recombinant Silk Produced in Mammalian Cells

2003 ◽  
Author(s):  
Costas N. Karatzas ◽  
Nathalie Chretien ◽  
François Duguay ◽  
Annie Bellemare ◽  
Jiang Feng Zhou ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Spider Silk ◽  
Silk Fibers ◽  
High Toughness

Tough synthetic spider-silk fibers obtained by titanium dioxide incorporation and formaldehyde cross-linking in a simple wet-spinning process

Biochimie ◽  
2020 ◽  
Vol 175 ◽  
pp. 77-84
Author(s):  
Hongnian Zhu ◽  
Yuan Sun ◽  
Tuo Yi ◽  
Suyang Wang ◽  
Junpeng Mi ◽  
...  
Keyword(s):  
Titanium Dioxide ◽  
Spider Silk ◽  
Wet Spinning ◽  
Cross Linking ◽  
Silk Fibers ◽  
Spinning Process

scholarly journals High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Axel Abelein ◽  
Gefei Chen ◽  
Kristīne Kitoka ◽  
Rihards Aleksis ◽  
Filips Oleskovs ◽  
...  
Keyword(s):  
Spider Silk ◽  
Amyloid Β ◽  
Silk Gland ◽  
High Yield ◽  
Efficient Production ◽  
Amyloid Β Peptide ◽  
Nephila Clavipes ◽  
Recombinant Production ◽  
Yield Production ◽  
High Yields

AbstractDuring storage in the silk gland, the N-terminal domain (NT) of spider silk proteins (spidroins) keeps the aggregation-prone repetitive region in solution at extreme concentrations. We observe that NTs from different spidroins have co-evolved with their respective repeat region, and now use an NT that is distantly related to previously used NTs, for efficient recombinant production of the amyloid-β peptide (Aβ) implicated in Alzheimer’s disease. A designed variant of NT from Nephila clavipes flagelliform spidroin, which in nature allows production and storage of β-hairpin repeat segments, gives exceptionally high yields of different human Aβ variants as a solubility tag. This tool enables efficient production of target peptides also in minimal medium and gives up to 10 times more isotope-labeled monomeric Aβ peptides per liter bacterial culture than previously reported.

scholarly journals Properties of Biomimetic Artificial Spider Silk Fibers Tuned by PostSpin Bath Incubation

Molecules ◽  
2020 ◽  
Vol 25 (14) ◽  
pp. 3248
Author(s):  
Gabriele Greco ◽  
Juanita Francis ◽  
Tina Arndt ◽  
Benjamin Schmuck ◽  
Fredrik G. Bäcklund ◽  
...  
Keyword(s):  
Spider Silk ◽  
Molecular Mechanisms ◽  
Efficient Production ◽  
Fiber Morphology ◽  
Silk Proteins ◽  
Silk Fibers ◽  
Aqueous Environments ◽  
Natural Counterpart ◽  
Phosphate Buffered Saline ◽  
Β Sheet

Efficient production of artificial spider silk fibers with properties that match its natural counterpart has still not been achieved. Recently, a biomimetic process for spinning recombinant spider silk proteins (spidroins) was presented, in which important molecular mechanisms involved in native spider silk spinning were recapitulated. However, drawbacks of these fibers included inferior mechanical properties and problems with low resistance to aqueous environments. In this work, we show that ≥5 h incubation of the fibers, in a collection bath of 500 mM NaAc and 200 mM NaCl, at pH 5 results in fibers that do not dissolve in water or phosphate buffered saline, which implies that the fibers can be used for applications that involve wet/humid conditions. Furthermore, incubation in the collection bath improved the strain at break and was associated with increased β-sheet content, but did not affect the fiber morphology. In summary, we present a simple way to improve artificial spider silk fiber strain at break and resistance to aqueous solvents.

scholarly journals The Nephila clavipes genome highlights the diversity of spider silk genes and their complex expression

2017 ◽  
Vol 49 (6) ◽  
pp. 895-903 ◽  
Author(s):  
Paul L Babb ◽  
Nicholas F Lahens ◽  
Sandra M Correa-Garhwal ◽  
David N Nicholson ◽  
Eun Ji Kim ◽  
...  
Keyword(s):  
Spider Silk ◽  
Nephila Clavipes ◽  
Complex Expression

scholarly journals Hybrid Spider Silk with Inorganic Nanomaterials

Nanomaterials ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1853
Author(s):  
Aleksandra P. Kiseleva ◽  
Grigorii O. Kiselev ◽  
Valeria O. Nikolaeva ◽  
Gulaim Seisenbaeva ◽  
Vadim Kessler ◽  
...  
Keyword(s):  
Hybrid Materials ◽  
High Performance ◽  
Spider Silk ◽  
Inorganic Compounds ◽  
Silk Fibers ◽  
Surface Areas ◽  
Macro Scale ◽  
Performance Functional ◽  
Inorganic Nanomaterials ◽  
Functional Components

High-performance functional biomaterials are becoming increasingly requested. Numerous natural and artificial polymers have already demonstrated their ability to serve as a basis for bio-composites. Spider silk offers a unique combination of desirable aspects such as biocompatibility, extraordinary mechanical properties, and tunable biodegradability, which are superior to those of most natural and engineered materials. Modifying spider silk with various inorganic nanomaterials with specific properties has led to the development of the hybrid materials with improved functionality. The purpose of using these inorganic nanomaterials is primarily due to their chemical nature, enhanced by large surface areas and quantum size phenomena. Functional properties of nanoparticles can be implemented to macro-scale components to produce silk-based hybrid materials, while spider silk fibers can serve as a matrix to combine the benefits of the functional components. Therefore, it is not surprising that hybrid materials based on spider silk and inorganic nanomaterials are considered extremely promising for potentially attractive applications in various fields, from optics and photonics to tissue regeneration. This review summarizes and discusses evidence of the use of various kinds of inorganic compounds in spider silk modification intended for a multitude of applications. It also provides an insight into approaches for obtaining hybrid silk-based materials via 3D printing.

Structure of the N-terminal domain of Euprosthenops australis dragline silk suggests that conversion of spidroin dope to spider silk involves a conserved asymmetric dimer intermediate

2019 ◽  
Vol 75 (7) ◽  
pp. 618-627 ◽  
Author(s):  
Wangshu Jiang ◽  
Glareh Askarieh ◽  
Alexander Shkumatov ◽  
My Hedhammar ◽  
Stefan D. Knight
Keyword(s):  
Electrostatic Interactions ◽  
Spider Silk ◽  
Quaternary Structure ◽  
Nephila Clavipes ◽  
Trigger Mechanism ◽  
Dragline Silk ◽  
Terminal Domain ◽  
Structure Changes ◽  
Molecular Events ◽  
Asymmetric Dimer

Spider silk is a biomaterial with exceptional mechanical toughness, and there is great interest in developing biomimetic methods to produce engineered spider silk-based materials. However, the mechanisms that regulate the conversion of spider silk proteins (spidroins) from highly soluble dope into silk are not completely understood. The N-terminal domain (NT) of Euprosthenops australis dragline silk protein undergoes conformational and quaternary-structure changes from a monomer at a pH above 7 to a homodimer at lower pH values. Conversion from the monomer to the dimer requires the protonation of three conserved glutamic acid residues, resulting in a low-pH `locked' dimer stabilized by symmetric electrostatic interactions at the poles of the dimer. The detailed molecular events during this transition are still unresolved. Here, a 2.1 Å resolution crystal structure of an NT T61A mutant in an alternative, asymmetric, dimer form in which the electrostatic interactions at one of the poles are dramatically different from those in symmetrical dimers is presented. A similar asymmetric dimer structure from dragline silk of Nephila clavipes has previously been described. It is suggested that asymmetric dimers represent a conserved intermediate state in spider silk formation, and a revised `lock-and-trigger' mechanism for spider silk formation is presented.

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