Probing the Mysteries of Spider Silk’s Uncharacteristically High Thermal Diffusivity

Author(s):  
Troy Munro ◽  
Changhu Xing ◽  
Heng Ban ◽  
Cameron Copeland ◽  
Randolph Lewis

Spider silks exhibit excellent strength, stiffness, and toughness simultaneously, a feat unachievable in most synthetic, structural materials. It has recently been reported that the thermal conductivity of dragline silk is comparable to copper, which is uncharacteristically high for a biomaterial. In order to develop a fundamental understanding of the high thermal properties of spider silk, further research must be made to explore how the structure and organization of spider silk proteins affects heat transfer characteristics. Synthetically produced silks created from spider silk proteins obtained from transgenic sources can be used to determine these protein structure effects by varying protein content and process treatments. This initial study determined the thermal properties of synthetic spider silk created from transgenic goat’s milk proteins using the transient electrothermal method (TET). Results show that the thermal properties of the synthetic silk are lower than the natural spider silk but vary based on the process treatment, and that the annealing of the gold film coated on the fiber has no effect on the measured thermal properties. These results provide a framework for further research on the protein content effect and its role in thermal properties.

Author(s):  
Troy Munro ◽  
Changhu Xing ◽  
Andrew Marquette ◽  
Heng Ban ◽  
Cameron Copeland ◽  
...  

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.


2020 ◽  
Author(s):  
Daniela Bittencourt ◽  
Paula F. Oliveira ◽  
Betulia M. Souto ◽  
Sonia Maria de Freitas ◽  
Valquiria Michalczechen-Lacerda ◽  
...  

<p>In order to better understand the relationship between the elastomeric behavior of Flagelliform (Flag) spider silks and its molecular structure, it was designed and produced the <i>Nephilengys cruentata</i> Flageliform (Flag) spidroin analogue rNcFlag2222. The recombinant proteins are composed by the elastic repetitive glycine-rich motifs (GPGGX/GGX) and the spacer region, rich in hydrophilic charged amino acids, present at the native silk spidroin. Using different approaches for nanomolecular protein analysis, the structural data of rNcFlag2222 recombinant proteins were compared in its fibrillar and in its fully solvated states. Based on the results and previous published data, it was possible to propose a model for the molecular dynamics of Flag spidroins’ repetitive core, during gland storage and fiber formation, and their contribution to its exceptional mechanoelastic properties. This model assumes that the Flag silk proteins acquire elastomeric behavior through a mechanism similar to collagen proteins, with the repetitive glycine-rich and the spacer regions, together with water, playing important roles in fiber assemble and elastomeric behavior.</p>


2020 ◽  
Vol 27 ◽  
Author(s):  
Fan Li ◽  
Chao Bian ◽  
Daiqin Li ◽  
Qiong Shi

: Spider silks have received extensive attention from scientists and industries around the world because of their remarkable mechanical properties, which include high tensile strength and extensibility. It is a leading-edge biomaterial resource, with a wide range of potential applications. Spider silks are composed of silk proteins, which are usually very large molecules, yet many silk proteins still remain largely underexplored. While there are numerous reviews on spider silks from diverse perspectives, here we provide a most up-to-date overview of the spider silk component protein family in terms of its molecular structure, evolution, hydrophobicity, and biomedical applications. Given the confusion regarding spidroin naming, we emphasize the need for coherent and consistent nomenclature for spidroins and provide recommendations for preexisting spidroin names that are inconsistent with nomenclature. We then review recent advances in the components, identification, and structures of spidroin genes. We next discuss the hydrophobicity of spidroins, with particular attention on the unique aquatic spider silks. Aquatic spider silks are less known but may inspire innovation in biomaterials. Furthermore, we provide new insights into antimicrobial peptides from spider silk glands. Finally, we present possibilities for future uses of spider silks.


2020 ◽  
Author(s):  
Daniela Bittencourt ◽  
Paula F. Oliveira ◽  
Betulia M. Souto ◽  
Sonia Maria de Freitas ◽  
Valquiria Michalczechen-Lacerda ◽  
...  

<p>In order to better understand the relationship between the elastomeric behavior of Flagelliform (Flag) spider silks and its molecular structure, it was designed and produced the <i>Nephilengys cruentata</i> Flageliform (Flag) spidroin analogue rNcFlag2222. The recombinant proteins are composed by the elastic repetitive glycine-rich motifs (GPGGX/GGX) and the spacer region, rich in hydrophilic charged amino acids, present at the native silk spidroin. Using different approaches for nanomolecular protein analysis, the structural data of rNcFlag2222 recombinant proteins were compared in its fibrillar and in its fully solvated states. Based on the results and previous published data, it was possible to propose a model for the molecular dynamics of Flag spidroins’ repetitive core, during gland storage and fiber formation, and their contribution to its exceptional mechanoelastic properties. This model assumes that the Flag silk proteins acquire elastomeric behavior through a mechanism similar to collagen proteins, with the repetitive glycine-rich and the spacer regions, together with water, playing important roles in fiber assemble and elastomeric behavior.</p>


2021 ◽  
pp. 100114
Author(s):  
Tilman U. Esser ◽  
Vanessa T. Trossmann ◽  
Sarah Lentz ◽  
Felix B. Engel ◽  
Thomas Scheibel

2012 ◽  
Vol 13 (10) ◽  
pp. 3189-3199 ◽  
Author(s):  
Seth L. Young ◽  
Maneesh Gupta ◽  
Christoph Hanske ◽  
Andreas Fery ◽  
Thomas Scheibel ◽  
...  

2018 ◽  
Vol 115 (45) ◽  
pp. 11507-11512 ◽  
Author(s):  
Lucas R. Parent ◽  
David Onofrei ◽  
Dian Xu ◽  
Dillan Stengel ◽  
John D. Roehling ◽  
...  

Many natural silks produced by spiders and insects are unique materials in their exceptional toughness and tensile strength, while being lightweight and biodegradable–properties that are currently unparalleled in synthetic materials. Myriad approaches have been attempted to prepare artificial silks from recombinant spider silk spidroins but have each failed to achieve the advantageous properties of the natural material. This is because of an incomplete understanding of the in vivo spidroin-to-fiber spinning process and, particularly, because of a lack of knowledge of the true morphological nature of spidroin nanostructures in the precursor dope solution and the mechanisms by which these nanostructures transform into micrometer-scale silk fibers. Herein we determine the physical form of the natural spidroin precursor nanostructures stored within spider glands that seed the formation of their silks and reveal the fundamental structural transformations that occur during the initial stages of extrusion en route to fiber formation. Using a combination of solution phase diffusion NMR and cryogenic transmission electron microscopy (cryo-TEM), we reveal direct evidence that the concentrated spidroin proteins are stored in the silk glands of black widow spiders as complex, hierarchical nanoassemblies (∼300 nm diameter) that are composed of micellar subdomains, substructures that themselves are engaged in the initial nanoscale transformations that occur in response to shear. We find that the established micelle theory of silk fiber precursor storage is incomplete and that the first steps toward liquid crystalline organization during silk spinning involve the fibrillization of nanoscale hierarchical micelle subdomains.


Biomaterials ◽  
2012 ◽  
Vol 33 (28) ◽  
pp. 6650-6659 ◽  
Author(s):  
Stefanie Wohlrab ◽  
Susanne Müller ◽  
Andreas Schmidt ◽  
Stefanie Neubauer ◽  
Horst Kessler ◽  
...  

Author(s):  
J�ngst Tomasz ◽  
Schacht Kristin ◽  
Smolan Willi ◽  
Ewald Andrea ◽  
Scheibel Thomas ◽  
...  
Keyword(s):  

2019 ◽  
Vol 5 (8) ◽  
pp. 4023-4036 ◽  
Author(s):  
Thomas I. Harris ◽  
Chase A. Paterson ◽  
Farhad Farjood ◽  
Ian D. Wadsworth ◽  
Lori Caldwell ◽  
...  

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