Hierarchical fibers for water collection inspired by spider silk

Nanoscale ◽  
2019 ◽  
Vol 11 (33) ◽  
pp. 15448-15463 ◽  
Author(s):  
Wei Chen ◽  
Zhiguang Guo
Keyword(s):  
Spider Silk ◽  
Effective Strategy ◽  
Water Collection ◽  
Spider Silks

The “wet-rebuilt” process of spider silk is considered an effective strategy for water collection. In this review, we give an advanced perspective on the fabrication and water-collection mechanisms from natural spider silks to functional fibers.

scholarly journals Hierarchical spidroin micellar nanoparticles as the fundamental precursors of spider silks

2018 ◽  
Vol 115 (45) ◽  
pp. 11507-11512 ◽  
Author(s):  
Lucas R. Parent ◽  
David Onofrei ◽  
Dian Xu ◽  
Dillan Stengel ◽  
John D. Roehling ◽  
...  
Keyword(s):  
Liquid Crystalline ◽  
Spider Silk ◽  
Fiber Spinning ◽  
Fiber Formation ◽  
Natural Material ◽  
Physical Form ◽  
Spinning Process ◽  
Black Widow Spiders ◽  
Spider Silks

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.

scholarly journals Tensegrity Modelling and the High Toughness of Spider Dragline Silk

Nanomaterials ◽  
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.

scholarly journals Investigating the transverse optical structure of spider silk micro-fibers using quantitative optical microscopy

Nanophotonics ◽  
2017 ◽  
Vol 6 (1) ◽  
pp. 341-348 ◽  
Author(s):  
Douglas J. Little ◽  
Deb M. Kane
Keyword(s):  
Refractive Index ◽  
Electromagnetic Scattering ◽  
Spider Silk ◽  
Transverse Optical ◽  
Graded Index ◽  
Argiope Keyserlingi ◽  
Wavelength Scale ◽  
Index Contrast ◽  
Spider Silks ◽  
Optical Structure

AbstractThe transverse optical structure of two orb-weaver (family Araneidae) spider dragline silks was investigated using a variant of the inverse-scattering technique. Immersing the silks in a closely refractive index-matched liquid, the minimum achievable image contrast was greater than expected for an optically homogeneous silk, given what is currently known about the optical absorption of these silks. This “excess contrast” indicated the presence of transverse optical structure within the spider silk. Applying electromagnetic scattering theory to a transparent double cylinder, the minimum achievable irradiance contrast for the Plebs eburnus and Argiope keyserlingi dragline silks was determined to be consistent with step index refractive index contrasts of 1−4×10−4 and 6–7×10−4, respectively, supposing outer-layer thicknesses consistent with previous TEM studies (50 nm and 100 nm, respectively). The possibility of graded index refractive index contrasts within the spider silks is also discussed. This is the strongest evidence, to date, that there is a refractive index contrast associated with the layered morphology of spider silks and/or variation of proportion of nanocrystalline components within the spider silk structure. The method is more generally applicable to optical micro-fibers, including those with refractive index variations on a sub-wavelength scale.

Bioinspired Materials: Controlled Fabrication and Water Collection Ability of Bioinspired Artificial Spider Silks (Adv. Mater. 32/2011)

2011 ◽  
Vol 23 (32) ◽  
pp. 3607-3607
Author(s):  
Hao Bai ◽  
Jie Ju ◽  
Ruize Sun ◽  
Yuan Chen ◽  
Yongmei Zheng ◽  
...  
Keyword(s):  
Bioinspired Materials ◽  
Water Collection ◽  
Spider Silks

scholarly journals Spidroins and Silk Fibers of Aquatic Spiders

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Sandra M. Correa-Garhwal ◽  
Thomas H. Clarke ◽  
Marc Janssen ◽  
Luc Crevecoeur ◽  
Bryce N. McQuillan ◽  
...  
Keyword(s):  
Gene Family ◽  
Spider Silk ◽  
Silk Gland ◽  
Aquatic Environments ◽  
Rna Seq ◽  
Silk Fibers ◽  
Fibroin Gene ◽  
Terrestrial Environments ◽  
Orb Web ◽  
Spider Silks

Abstract Spiders are commonly found in terrestrial environments and many rely heavily on their silks for fitness related tasks such as reproduction and dispersal. Although rare, a few species occupy aquatic or semi-aquatic habitats and for them, silk-related specializations are also essential to survive in aquatic environments. Most spider silks studied to date are from cob-web and orb-web weaving species, leaving the silks from many other terrestrial spiders as well as water-associated spiders largely undescribed. Here, we characterize silks from three Dictynoidea species: the aquatic spiders Argyroneta aquatica and Desis marina as well as the terrestrial Badumna longinqua. From silk gland RNA-Seq libraries, we report a total of 47 different homologs of the spidroin (spider fibroin) gene family. Some of these 47 spidroins correspond to known spidroin types (aciniform, ampullate, cribellar, pyriform, and tubuliform), while other spidroins represent novel branches of the spidroin gene family. We also report a hydrophobic amino acid motif (GV) that, to date, is found only in the spidroins of aquatic and semi-aquatic spiders. Comparison of spider silk sequences to the silks from other water-associated arthropods, shows that there is a diversity of strategies to function in aquatic environments.

scholarly journals Spidroin-Based Biomaterials in Tissue Engineering: General Approaches and Potential Stem Cell Therapies

2021 ◽  
Vol 2021 ◽  
pp. 1-16
Author(s):  
Qi Zhang ◽  
Min Li ◽  
Wenbo Hu ◽  
Xin Wang ◽  
Jinlian Hu
Keyword(s):  
Tissue Engineering ◽  
Biomedical Applications ◽  
Spider Silk ◽  
Nerve Repair ◽  
Cartilage Regeneration ◽  
Genetically Engineered ◽  
Cell Therapies ◽  
Wide Range ◽  
Lung Tissue Engineering ◽  
Spider Silks

Spider silks are increasingly gaining interest for potential use as biomaterials in tissue engineering and biomedical applications. Owing to their facile and versatile processability in native and regenerated forms, they can be easily tuned via chemical synthesis or recombinant technologies to address specific issues required for applications. In the past few decades, native spider silk and recombinant silk materials have been explored for a wide range of applications due to their superior strength, toughness, and elasticity as well as biocompatibility, biodegradation, and nonimmunogenicity. Herein, we present an overview of the recent advances in spider silk protein that fabricate biomaterials for tissue engineering and regenerative medicine. Beginning with a brief description of biological and mechanical properties of spidroin-based materials and the cellular regulatory mechanism, this review summarizes various types of spidroin-based biomaterials from genetically engineered spider silks and their prospects for specific biomedical applications (e.g., lung tissue engineering, vascularization, bone and cartilage regeneration, and peripheral nerve repair), and finally, we prospected the development direction and manufacturing technology of building more refined and customized spidroin-based protein scaffolds.

scholarly journals Post-secretion processing influences spider silk performance

2012 ◽  
Vol 9 (75) ◽  
pp. 2479-2487 ◽  
Author(s):  
Sean J. Blamires ◽  
Chung-Lin Wu ◽  
Todd A. Blackledge ◽  
I-Min Tso
Keyword(s):  
Mechanical Properties ◽  
Amino Acid ◽  
Ground State ◽  
Spider Silk ◽  
Mechanical Performance ◽  
Protein Composition ◽  
Compositional Changes ◽  
Spinning Speed ◽  
Spider Silks ◽  
Β Sheet

Phenotypic variation facilitates adaptations to novel environments. Silk is an example of a highly variable biomaterial. The two-spidroin (MaSp) model suggests that spider major ampullate (MA) silk is composed of two proteins—MaSp1 predominately contains alanine and glycine and forms strength enhancing β-sheet crystals, while MaSp2 contains proline and forms elastic spirals. Nonetheless, mechanical properties can vary in spider silks without congruent amino acid compositional changes. We predicted that post-secretion processing causes variation in the mechanical performance of wild MA silk independent of protein composition or spinning speed across 10 species of spider. We used supercontraction to remove post-secretion effects and compared the mechanics of silk in this ‘ground state’ with wild native silks. Native silk mechanics varied less among species compared with ‘ground state’ silks. Variability in the mechanics of ‘ground state’ silks was associated with proline composition. However, variability in native silks did not. We attribute interspecific similarities in the mechanical properties of native silks, regardless of amino acid compositions, to glandular processes altering molecular alignment of the proteins prior to extrusion. Such post-secretion processing may enable MA silk to maintain functionality across environments, facilitating its function as a component of an insect-catching web.

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.

Nephila Clavipes Dragline Silk: Approaches to a Recombinantly Produced Silk Protein

1993 ◽  
Vol 330 ◽  
Author(s):  
Charlene M. Mello ◽  
Steven Arcidiacono ◽  
Richard Beckwitt ◽  
John Prince ◽  
Kris Senecal ◽  
...  
Keyword(s):  
High Performance ◽  
Spider Silk ◽  
Recombinant Dna ◽  
Electromagnetic Spectrum ◽  
Nephila Clavipes ◽  
Natural Function ◽  
High Performance Fiber ◽  
Recombinant Dna Techniques ◽  
Clone And Express ◽  
Spider Silks

Spider silks exhibit an unusual combination of strength and toughness that distinguishes them from other natural and synthetic fibers. Silk proteins perform a key natural function as structural fibers, to absorb impact energy from flying insects without breaking. They dissipate energy over a broad area and balance stiffness, strength and extensibility (1,2). In addition to their unusual mechanical properties and visual lustre, silks also exhibit interesting interference patterns within the electromagnetic spectrum (3), unusual viscometric patterns related to processing (4), and piezoelectric properties (3,5,6). These properties suggest they would be good candidates for high performance fiber and composite applications. However, the spider is not capable of producing sufficient quantities of proteins to enable thorough evaluation of their potential. Consequently, we are pursuing recombinant DNA techniques to clone and express adequate quantities of recombinant spider silk for these studies.

Critical role of minor eggcase silk component in promoting spidroin chain alignment and strong fiber formation

2021 ◽  
Vol 118 (38) ◽  
pp. e2100496118
Author(s):  
Tiantian Fan ◽  
Ruiqi Qin ◽  
Yan Zhang ◽  
Jingxia Wang ◽  
Jing-Song Fan ◽  
...  
Keyword(s):  
Self Assembly ◽  
Spider Silk ◽  
Critical Role ◽  
Minor Component ◽  
Fiber Formation ◽  
Repetitive Domain ◽  
Chain Alignment ◽  
Main Components ◽  
Spider Silks

Natural spider silk with extraordinary mechanical properties is typically spun from more than one type of spidroin. Although the main components of various spider silks have been widely studied, little is known about the molecular role of the minor silk components in spidroin self-assembly and fiber formation. Here, we show that the minor component of spider eggcase silk, TuSp2, not only accelerates self-assembly but remarkably promotes molecular chain alignment of spidroins upon physical shearing. NMR structure of the repetitive domain of TuSp2 reveals that its dimeric structure with unique charged surface serves as a platform to recruit different domains of the main eggcase component TuSp1. Artificial fiber spun from the complex between TuSp1 and TuSp2 minispidroins exhibits considerably higher strength and Young’s modulus than its native counterpart. These results create a framework for rationally designing silk biomaterials based on distinct roles of silk components.

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