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Adele Peters in her October 31, 2019 article for Fast Company describes the technology used to make this jacket,
A typical waterproof winter jacket is made with nylon—a material that, like other plastics, is made from petroleum. But a new limited-edition jacket from The North Face Japan uses something called “brewed protein” instead. It’s a material inspired by spider silk that is fermented in giant vats, the same way that breweries make beer.
It’s one of the first uses of a material produced by the Japanese startup Spiber, a company that has spent more than a decade developing a new process to make high-performance textiles and other products that don’t rely on fossil fuels, animals, or natural fibers like cotton, all of which have environmental issues. …
The company designs genes that code for a specific protein—the first was an exact replica of natural spider silk, known for its extreme strength—and then introduces the genes into microorganisms that can produce the protein efficiently. Inside giant tanks, the microorganisms are fed sugar, grow and multiply, and produce the protein through fermentation. …
Spiber first started collaborating with Goldwin, a Japanese outdoor brand that owns the Japanese rights to The North Face, in 2015, and created an early prototype of a jacket then. But it quickly realized that an exact replica of spider silk wouldn’t work well for the application; the material sucks up water, and the jacket needed to be waterproof.
“We spent the last four years going back to the drawing board, redesigning our protein molecule—the very order of the amino acids in the molecule,” says Meyer [Daniel Meyer, Spiber’s head of corporate global marketing]. “And we created our own hydrophobic [water repellent] version of spider silk. It’s inspired by natural spider silk, but we have made our own design changes such that it would be more hydrophobic and meet the performance requirements of The North Face Japan.”
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The jacket is available for purchase but only by a lottery, which has now closed. According to Peters, a large, commercial production facility is being built in Thailand so that at some point a Moon Parka will be affordable. For reference, the lottery jackets were priced at ¥150,000 (about $1,377 US).
You can find Spiber here in mid-March [2020] according to the homepage.
Caption: An orb spider, glue-maker extraordinaire, at work on a web. Credit: The University of Akron
Scientists are taking inspiration from spiders in their quest to develop better adhesives. (Are they abandoning the gecko? Usually when scientists study adhesiveness, there’s talk of geckos. From a June 5, 2018 news item on ScienceDaily,
Ever wonder why paint peels off the wall during summer’s high humidity? It’s the same reason that bandages separate from skin when we bathe or swim.
Interfacial water, as it’s known, forms a slippery and non-adhesive layer between the glue and the surface to which it is meant to stick, interfering with the formation of adhesive bonds between the two.
Overcoming the effects of interfacial water is one of the challenges facing developers of commercial adhesives.
To find a solution, researchers at The University of Akron (UA) are looking to one of the strongest materials found in nature: spider silk.
The sticky glue that coats the silk threads of spider webs is a hydrogel, meaning it is full of water. One would think, then, that spiders would have difficulty catching prey, especially in humid conditions — but they do not. In fact, their sticky glue, which has been a subject of intensive research for years, is one of the most effective biological glues in all of nature.
So how is spider glue able to stick in highly humid conditions?
That question was the subject of investigation by UA graduate students Saranshu Singla, Gaurav Amarpuri and Nishad Dhopatkar, who have been working with Dr. Ali Dhinojwala, interim dean of the College of Polymer Science and Polymer Engineering, and Dr. Todd Blackledge, professor of biology in the Integrated Bioscience program. Both professors are principal investigators in UA’s Biomimicry Research Innovation Center [BRIC], which specializes in emulating biological forms, processes, patterns and systems to solve technical challenges.
The team’s findings, which may provide the clue to developing stronger commercial adhesives, can be read in a paper recently published in the journal Nature Communications.
Singla and her colleagues set out to examine the secret behind the success of the common orb spider (Larinioides cornutus) glue and uncover how it overcomes the primary obstacle of achieving good adhesion in the humid conditions where water could be present between the glue and the target surface.
To investigate the processes involved, the team took orb spider glue, set it on sapphire substrate, then examined it using a combination of interface-sensitive spectroscopy and infrared spectroscopy.
Spider glue is made of three elements: two specialized glycoproteins, a collection of low molecular mass organic and inorganic compounds (LMMCs), and water. The LMMCs are hygroscopic (water-attracting), which keeps the glue soft and tacky to stick.
Singla and her team discovered that these glycoproteins act as primary binding agents to the surface. Glycoprotein-based glues have been identified in several other biological glues, such as fungi, algae, diatoms, sea stars, sticklebacks and English ivy.
But why doesn’t the water present in the spider glue interfere with the adhesive contact the way it does with most synthetic adhesives?
The LMMCs, the team concluded, perform a previously unknown function of sequestering interfacial water, preventing adhesive failure.
Singla and colleagues determined that it is the interaction of glycoproteins and LMMCs that governs the adhesive quality of the glue produced, with the respective proportions varying across species, thus optimizing adhesive strength to match the relative humidity of spider habitat.
“The hygroscopic compounds – known as water-absorbers – in spider glue play a previously unknown role in moving water away from the boundary, thereby preventing failure of spider glue at high humidity,” explained Singla.
The ability of the spider glue to overcome the problem of interfacial water by effectively absorbing it is the key finding of the research, and the one with perhaps the strongest prospect for commercial development.
“Imagine a paint that is guaranteed for life, come rain or shine,” Singla remarked.
All thanks to your friendly neighborhood spider glue.
Researcher Bor-Kai Hsiung’s work has graced this blog before but the topic was tarantulas and their structural colour. This time, it’s all about Australian peacock spiders and their structural colour according to a December 22, 2017 news item on ScienceDaily,
Even if you are arachnophobic, you probably have seen pictures or videos of Australian peacock spiders (Maratus spp.). These tiny spiders are only 1-5 mm long but are famous for their flamboyant courtship displays featuring diverse and intricate body colorations, patterns, and movements.
The spiders extremely large anterior median eyes have excellent color vision and combine with their bright colors to make peacock spiders cute enough to cure most people of their arachnophobia. But these displays aren’t just pretty to look at, they also inspire new ways for humans to produce color in technology.
One species of peacock spider — the rainbow peacock spider (Maratus robinsoni) is particularly neat, because it showcases an intense rainbow iridescent signal in males’ courtship displays to the females. This is the first known instance in nature of males using an entire rainbow of colors to entice females. Dr. Bor-Kai Hsiung led an international team of researchers from the US (UAkron, Cal Tech, UC San Diego, UNL [University of Nebraska-Lincoln]), Belgium (Ghent University), Netherlands (UGroningen), and Australia to discover how rainbow peacock spiders produce this unique multi-color iridescent signal.
Using a diverse array of research techniques, including light and electron microscopy, hyperspectral imaging, imaging scatterometry, nano 3D printing and optical modeling, the team found the origin of this intense rainbow iridescence emerged from specialized abdominal scales of the spiders. These scales have an airfoil-like microscopic 3D contour with nanoscale diffraction grating structures on the surface.
The interaction between the surface nano-diffraction grating and the microscopic curvature of the scales enables separation and isolation of light into its component wavelengths at finer angles and smaller distances than are possible with current manmade engineering technologies.
Inspiration from these super iridescent scales can be used to overcome current limitations in spectral manipulation, and to further reduce the size of optical spectrometers for applications where fine-scale spectral resolution is required in a very small package, notably instruments on space missions, or wearable chemical detection systems. And it could have a wide array of implications to fields ranging from life sciences and biotechnologies to material sciences and engineering.
Here’s a video of an Australian rainbow peacock spider,
Here’s more from the YouTube description published on April 13, 2017 by Peacockspiderman,
Scenes of Maratus robinsoni, a spider Peter Robinson discovered and David Hill and I named it after him in 2012. You can read our description on pages 36-41 in Peckhamia 103.2, which can be downloaded from the Peckhamia website http://peckhamia.com/peckhamia_number…. This is one of the two smallest species of peacock spider (2.5 mm long) and the only spider we know of in which colour changes occur every time it moves, this video was created to document this. Music: ‘Be Still’ by Johannes Bornlöf licensed through my MCN ‘Brave Bison’ from ‘Epidemic Sound’ For licensing inquiries please contact Brave Bison licensing@bravebison.io
The University of California at San Diego also published a December 22, 2017 news release about this work, which covers some of the same ground while providing a few new tidbits of information,
Brightly colored Australian peacock spiders (Maratus spp.) captivate even the most arachnophobic viewers with their flamboyant courtship displays featuring diverse and intricate body colorations, patterns, and movements – all packed into miniature bodies measuring less than five millimeters in size for many species. However, these displays are not just pretty to look at. They also inspire new ways for humans to produce color in technology.
One species of peacock spider – the rainbow peacock spider (Maratus robinsoni) – is particularly impressive, because it showcases an intense rainbow iridescent signal in males’ courtship displays to females. This is the first known instance in nature of males using an entire rainbow of colors to entice females to mate. But how do males make their rainbows? A new study published in Nature Communications looked to answer that question.
Figuring out the answers was inherently interdisciplinary so Bor-Kai Hsiung, a postdoctoral scholar at Scripps Institution of Oceanography at the University of California San Diego, assembled an international team that included biologists, physicists and engineers. Starting while he was a Ph.D. student at The University of Akron under the mentorship of Todd Blackledge and Matthew Shawkey, the team included researchers from UA, Scripps Oceanography, California Institute of Technology, and University of Nebraska-Lincoln, the University of Ghent in Belgium, University of Groningen in Netherlands, and Australia to discover how rainbow peacock spiders produce this unique iridescent signal.
The team investigated the spider’s photonic structures using techniques that included light and electron microscopy, hyperspectral imaging, imaging scatterometry and optical modeling to generate hypotheses about how the spider’s scale generate such intense rainbows. The team then used cutting-edge nano 3D printing to fabricate different prototypes to test and validate their hypotheses. In the end, they found that the intense rainbow iridescence emerged from specialized abdominal scales on the spiders. These scales combine an airfoil-like microscopic 3D contour with nanoscale diffraction grating structures on the surface. It is the interaction between the surface nano-diffraction grating and the microscopic curvature of the scales that enables separation and isolation of light into its component wavelengths at finer angles and smaller distances than are possible with current engineering technologies.
“Who knew that such a small critter would create such an intense iridescence using extremely sophisticated mechanisms that will inspire optical engineers,” said Dimitri Deheyn, Hsuing’s advisor at Scripps Oceanography and a coauthor of the study.
For Hsiung, the finding wasn’t quite so unexpected.
“One of the main questions that I wanted to address in my Ph.D. dissertation was ‘how does nature modulate iridescence?’ From a biomimicry perspective, to fully understand and address a question, one has to take extremes from both ends into consideration. I purposefully chose to study these tiny spiders with intense iridescence after having investigated the non-iridescent blue tarantulas,” said Hsiung.
The mechanism behind these tiny rainbows may inspire new color technology, but would not have been discovered without research combining basic natural history with physics and engineering, the researchers said.
“Nanoscale 3D printing allowed us to experimentally validate our models, which was really exciting,” said Shawkey. “We hope that these techniques will become common in the future.”
“As an engineer, what I found fascinating about these spider structural colors is how these long evolved complex structures can still outperform human engineering,” said Radwanul Hasan Siddique, a postdoctoral scholar at Caltech and study coauthor. “Even with high-end fabrication techniques, we could not replicate the exact structures. I wonder how the spiders assemble these fancy structural patterns in the first place!”
Inspiration from these super iridescent spider scales can be used to overcome current limitations in spectral manipulation, and to reduce the size of optical spectrometers for applications where fine-scale spectral resolution is required in a very small package, notably instruments on space missions, or wearable chemical detection systems.
In the end, peacock spiders don’t just produce nature’s smallest rainbows.They could also have implications for a wide array of fields ranging from life sciences and biotechnologies to material sciences and engineering.
Before citing the paper and providing a link, here’s a story by Robert F. Service for Science magazine about attempts to capitalize on ‘spider technology’, in this case spider silk,
The hype over spider silk has been building since 1710. That was the year François Xavier Bon de Saint Hilaire, president of the Royal Society of Sciences in Montpellier, France, wrote to his colleagues, “You will be surpriz’d to hear, that Spiders make a Silk, as beautiful, strong and glossy, as common Silk.” Modern pitches boast that spider silk is five times stronger than steel yet more flexible than rubber. If it could be made into ropes, a macroscale web would be able to snare a jetliner.
The key word is “if.” Researchers first cloned a spider silk gene in 1990, in hopes of incorporating it into other organisms to produce the silk. (Spiders can’t be farmed like silkworms because they are territorial and cannibalistic.) Today, Escherichia coli bacteria, yeasts, plants, silkworms, and even goats have been genetically engineered to churn out spider silk proteins, though the proteins are often shorter and simpler than the spiders’ own. Companies have managed to spin those proteins into enough high-strength thread to produce a few prototype garments, including a running shoe by Adidas and a lightweight parka by The North Face. But so far, companies have struggled to mass produce these supersilks.
Some executives say that may finally be about to change. One Emeryville, California-based startup, Bolt Threads, says it has perfected growing spider silk proteins in yeast and is poised to turn out tons of spider silk thread per year. In Lansing, Michigan, Kraig Biocraft Laboratories says it needs only to finalize negotiations with silkworm farms in Vietnam to produce mass quantities of a combination spider/silkworm silk, which the U.S. Army is now testing for ballistics protection. …
I encourage you to read Service’s article in its entirety if the commercialization prospects for spider silk interest you as it includes gems such as this,
Spider silk proteins are already making their retail debut—but in cosmetics and medical devices, not high-strength fibers. AMSilk grows spider silk proteins in E. coli and dries the purified protein into powders or mixes it into gels, for use as additives for personal care products, such as moisture-retaining skin lotions. The silk proteins supposedly help the lotions form a very smooth, but breathable, layer over the skin. Römer says the company now sells tons of its purified silk protein ingredients every year.
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Finally, here’s a citation for and a link to the paper about Australian peacock spiders and nanophotonics,
Rainbow peacock spiders inspire miniature super-iridescent optics by Bor-Kai Hsiung, Radwanul Hasan Siddique, Doekele G. Stavenga, Jürgen C. Otto, Michael C. Allen, Ying Liu, Yong-Feng Lu, Dimitri D. Deheyn, Matthew D. Shawkey, & Todd A. Blackledge. Nature Communications 8, Article number: 2278 (2017) doi:10.1038/s41467-017-02451-x Published online: 22 December 2017
… researchers in Italy and the UK have found a way to make Spidey’s silk a lot stronger, using various different spider species and carbon nanotubes or graphene.
The research team, led by Professor Nicola Pugno at the University of Trento, Italy, succeeded in having their spiders produce silk with up to three times the strength and ten times the toughness of the regular material.
Their discovery, published today in the journal 2D Materials, could pave the way for a new class of bionicomposites, with a wide variety of uses.
Professor Pugno said: “Humans have used silkworm silks widely for thousands of years, but recently research has focussed on spider silk, as it has extremely promising mechanical properties. It is among the best spun polymer fibres in terms of tensile strength, ultimate strain, and especially toughness, even when compared to synthetic fibres such as Kevlar.
“We already know that there are biominerals present in in the protein matrices and hard tissues of insects, which gives them high strength and hardness in their jaws, mandibles and teeth, for example. So our study looked at whether spider silk’s properties could be ‘enhanced’ by artificially incorporating various different nanomaterials into the silk’s biological protein structures.”
To do this, the team exposed three different spider species to water dispersions containing carbon nanotubes or graphene.
After collecting the spiders’ silk, the team tested its tensile strength and toughness.
Professor Pugno said: “We found that the strongest silk the spiders spun had a fracture strength up to 5.4 gigapascals (GPa), and a toughness modulus up to 1,570 joules per gram (J/g). Normal spider silk, by comparison, has a fracture strength of around 1.5 GPa and a toughness modulus of around 150 J/g.
“This is the highest fibre toughness discovered to date, and a strength comparable to that of the strongest carbon fibres or limpet teeth. These are still early days, but our results are a proof of concept that paves the way to exploiting the naturally efficient spider spinning process to produce reinforced bionic silk fibres, thus further improving one of the most promising strong materials.
“These silks’ high toughness and resistance to ultimate strain could have applications such as parachutes.”
“Furthermore, this process of the natural integration of reinforcements in biological structural materials could also be applied to other animals and plants, leading to a new class of “bionicomposites” for innovative applications.”
Remember this? “You are what you eat.” If you’ve ever had doubts about that saying, these spiders should be laying them to rest.
Sadly, this news release doesn’t explain much about the decision to feed the spiders graphene or carbon nanotubes, which are identical other than in their respective shapes (sheet vs tube) and whether those shapes did or did not affect the strength of the silk.
Here’s a link to and a citation for the paper,
Spider silk reinforced by graphene or carbon nanotubes by Emiliano Lepore, Federico Bosia, Francesco Bonaccorso, Matteo Bruna, Simone Taioli, Giovanni Garberoglio, Andrea C Ferrari, and Nicola Maria Pugno. 2D Materials, Volume 4, Number 3 DOI: https://doi.org/10.1088/2053-1583/aa7cd3 Published 14 August 2017
Pugno was most recently mentioned here in a May 29, 2015 posting where he was listed as an author for a paper on synthesizing spider silk. Prior to 2015 I was familiar with Pugno’s name due to his work on adhesiveness in geckos.
I have a couple of questions, what is ‘click’ chemistry and how does a chance meeting lead to a five-year, interdisciplinary research project on synthetic spider silk? From a Jan. 4, 2017 news item on ScienceDaily,
A chance meeting between a spider expert and a chemist has led to the development of antibiotic synthetic spider silk.
After five years’ work an interdisciplinary team of scientists at The University of Nottingham has developed a technique to produce chemically functionalised spider silk that can be tailored to applications used in drug delivery, regenerative medicine and wound healing.
The Nottingham research team has shown for the first time how ‘click-chemistry’ can be used to attach molecules, such as antibiotics or fluorescent dyes, to artificially produced spider silk synthesised by E.coli bacteria. The research, funded by the Biotechnology and Biological Sciences Research Council (BBSRC) is published today in the online journal Advanced Materials.
The chosen molecules can be ‘clicked’ into place in soluble silk protein before it has been turned into fibres, or after the fibres have been formed. This means that the process can be easily controlled and more than one type of molecule can be used to ‘decorate’ individual silk strands.
Nottingham breakthrough
In a laboratory in the Centre of Biomolecular Sciences, Professor Neil Thomas from the School of Chemistry in collaboration with Dr Sara Goodacre from the School of Life Sciences, has led a team of BBSRC DTP-funded PhD students starting with David Harvey who was then joined by Victor Tudorica, Leah Ashley and Tom Coekin. They have developed and diversified this new approach to functionalising ‘recombinant’ — artificial — spider silk with a wide range of small molecules.
They have shown that when these ‘silk’ fibres are ‘decorated’ with the antibiotic levofloxacin it is slowly released from the silk, retaining its anti-bacterial activity for at least five days.
Neil Thomas, a Professor of Medicinal and Biological Chemistry, said: “Our technique allows the rapid generation of biocompatible, mono or multi-functionalised silk structures for use in a wide range of applications. These will be particularly useful in the fields of tissue engineering and biomedicine.”
Remarkable qualities of spider silk
Spider silk is strong, biocompatible and biodegradable. It is a protein-based material that does not appear to cause a strong immune, allergic or inflammatory reaction. With the recent development of recombinant spider silk, the race has been on to find ways of harnessing its remarkable qualities.
The Nottingham research team has shown that their technique can be used to create a biodegradable mesh which can do two jobs at once. It can replace the extra cellular matrix that our own cells generate, to accelerate growth of the new tissue. It can also be used for the slow release of antibiotics.
Professor Thomas said: “There is the possibility of using the silk in advanced dressings for the treatment of slow-healing wounds such as diabetic ulcers. Using our technique infection could be prevented over weeks or months by the controlled release of antibiotics. At the same time tissue regeneration is accelerated by silk fibres functioning as a temporary scaffold before being biodegraded.”
The medicinal properties of spider silk recognised for centuries.
The medicinal properties of spider silk have been recognised for centuries but not clearly understood. The Greeks and Romans treated wounded soldiers with spider webs to stop bleeding. It is said that soldiers would use a combination of honey and vinegar to clean deep wounds and then cover the whole thing with balled-up spider webs.
There is even a mention in Shakespeare’s Midsummer Night’s Dream: “I shall desire you of more acquaintance, good master cobweb,” the character ‘Bottom’ said. “If I cut my finger, I shall make bold of you.”
The press release goes on to describe the genesis of the project and how this multidisciplinary team was formed in more detail,
The idea came together at a discipline bridging university ‘sandpit’ meeting five years ago. Dr Goodacre says her chance meeting at that event with Professor Thomas proved to be one of the most productive afternoons of her career.
Dr Goodacre, who heads up the SpiderLab in the School of Life Sciences, said: “I got up at that meeting and showed the audience a picture of some spider silk. I said ‘I want to understand how this silk works, and then make some.’
“At the end of the session Neil came up to me and said ‘I think my group could make that.’ He also suggested that there might be more interesting ‘tweaks’ one could make so that the silk could be ‘decorated’ with different, useful, compounds either permanently or which could be released over time due to a change in the acidity of the environment.”
The approach required the production of the silk proteins in a bacterium where an amino acid not normally found in proteins was included. This amino acid contained an azide group which is widely used in ‘click’ reactions that only occur at that position in the protein. It was an approach that no-one had used before with spider silk — but the big question was — would it work?
Dr Goodacre said: “It was the start of a fascinating adventure that saw a postdoc undertake a very preliminary study to construct the synthetic silks. He was a former SpiderLab PhD student who had previously worked with our tarantulas. Thanks to his ground work we showed we could produce the silk proteins in bacteria. We were then joined by David Harvey, a new PhD student, who not only made the silk fibres, incorporating the unusual amino acid, but also decorated it and demonstrated its antibiotic activity. He has since extended those first ideas far beyond what we had thought might be possible.”
David Harvey’s work is described in this paper but Professor Thomas and Dr Goodacre say this is just the start. There are other joint SpiderLab/Thomas lab students working on uses for this technology in the hope of developing it further.
David Harvey, the lead author on this their first paper, has just been awarded his PhD and is now a postdoctoral researcher on a BBSRC follow-on grant so is still at the heart of the research. His current work is focused on driving the functionalised spider silk technology towards commercial application in wound healing and tissue regeneration.
I imagine Mr. Cockayne’s name has led to much teasing over the years. People who have names with that kind of potential tend to either change them or double down and refuse to compromise.
Bangor University (Wales, UK) is making quite the impact these days. I’d never heard of the institution until their breakthrough with nanobeads (Sept. 7, 2016 posting) to break through a resolution barrier and now there’s a second breakthrough with their partners at Oxford University (England, UK). From an Aug. 19, 2016 news item on ScienceDaily (Note: A link has been removed),
Scientists at the UK’s Bangor and Oxford universities have achieved a world first: using spider-silk as a superlens to increase the microscope’s potential.
Extending the limit of classical microscope’s resolution has been the ‘El Dorado’ or ‘Holy Grail’ of microscopy for over a century. Physical laws of light make it impossible to view objects smaller than 200 nm — the smallest size of bacteria, using a normal microscope alone. However, superlenses which enable us to see beyond the current magnification have been the goal since the turn of the millennium.
Hot on the heels of a paper (Sci. Adv. 2 e1600901,2016) revealing that a team at Bangor University’s School of Electronic Engineering has used a nanobead-derived superlens to break the perceived resolution barrier, the same team has achieved another world first.
Now the team, led by Dr Zengbo Wang and in colloboration with Prof. Fritz Vollrath’s silk group at Oxford University’s Department of Zoology, has used a naturally occurring material — dragline silk of the golden web spider, as an additional superlens, applied to the surface of the material to be viewed, to provide an additional 2-3 times magnification.
This is the first time that a naturally occurring biological material has been used as a superlens.
In the paper in Nano Letters (DOI: 10.1021/acs.nanolett.6b02641, Aug 17 2016), the joint team reveals how they used a cylindrical piece of spider silk from the thumb sized Nephila spider as a lens.
Dr Zengbo Wang said:
“We have proved that the resolution barrier of microscope can be broken using a superlens, but production of manufactured superlenses invovles some complex engineering processes which are not widely accessible to other reserchers. This is why we have been interested in looking for naturally occurring superlenses provided by ‘Mother Nature’, which may exist around us, so that everyone can access superlenses.”
Prof Fritz Vollrath adds:
“It is very exciting to find yet another cutting edge and totally novel use for a spider silk, which we have been studying for over two decades in my laboratory.”
These lenses could be used for seeing and viewing previously ‘invisible’ structures, including engineered nano-structures and biological micro-structures as well as, potentially, native germs and viruses.
The natural cylindrical structure at a micron- and submicron-scale make silks ideal candidates, in this case, the individual filaments had diameters of one tenth of a thin human hair.
The spider filament enabled the group to view details on a micro-chip and a blue- ray disk which would be invisible using the unmodified optical microscope.
In much the same was as when you look through a cylindrical glass or bottle, the clearest image only runs along the narrow strip directly opposite your line of vision, or resting on the surface being viewed, the single filament provides a one dimensional viewing image along its length.
Wang explains:
“The cylindrical silk lens has advantages in the larger field-of-view when compared to a microsphere superlens. Importantly for potential commercial applications, a spider silk nanoscope would be robust and economical, which in turn could provide excellent manufacturing platforms for a wide range of applications.”
James Monks, a co-author on the paper comments: “it has been an exciting time to be able to develop this project as part of my honours degree in electronic engineering at Bangor University and I am now very much looking forward to joining Dr Wang’s team as a PhD student in nano-photonics.”
The researchers have provided a close up image with details,
Caption: (a) Nephila edulis spider in its web. (b) Schematic drawing of reflection mode silk biosuperlens imaging. The spider silk was placed directly on top of the sample surface by using a soft tape, which magnify underlying nano objects 2-3 times (c) SEM image of Blu-ray disk with 200/100 nm groove and lines (d) Clear magnified image (2.1x) of Blu-ray disk under spider silk superlens. Credit: Bangor University/ University of Oxford
Here’s a link to and a citation for the ‘spider silk’ superlens paper,
Spider Silk: Mother Nature’s Bio-Superlens by James N. Monks, Bing Yan, Nicholas Hawkins, Fritz Vollrath, and Zengbo Wang. Nano Lett., Article ASAP DOI: 10.1021/acs.nanolett.6b02641 Publication Date (Web): August 17, 2016
On May 21 [2016], Department of Civil and Environmental Engineering head and McAfee Professor of Engineering Markus J. Buehler received the 2015 Foresight Institute Feynman Prize in Theoretical Molecular Nanotechnology. Buehler’s award was one of three prizes presented by the Foresight Institute, a leading think tank and public interest organization, at its annual conference in Palo Alto, California. …
…
The Foresight Institute recognized Buehler for his important contributions to making nanotechnology scalable for large-scale materials applications, enabled by bottom-up multiscale computational methods, and linking new manufacturing and characterization methods.
Focusing on mechanical properties — especially deformation and failure — and translation from biological materials and structures to bio-inspired synthetic materials, his work has led to the development and application of new modeling, design, and manufacturing approaches for advanced materials that offer greater resilience and a wide range of controllable properties from the nano- to the macroscale.
Buehler’s signature achievement, according to the Institute, is the application of molecular and chemical principles in the analysis of mechanical systems, with the aim to design devices and materials that provide a defined set of functions.
“It’s an incredible honor to receive such an esteemed award. I owe this to the outstanding students and postdocs whom I had a pleasure to work with over the years, my colleagues, as well my own mentors,” Buehler said. “Richard Feynman was a revolutionary scientist of his generation. It’s a privilege to share his goals of researching molecular technology at very small scale to create new, more efficient, and better lasting materials at much larger scale that will help transform lives and industries.”
The two other award winners are Professor Michelle Y. Simmons of the University of New South Wales [Australia], who won the Feynman Prize for Experimental Molecular Nanotechnology, and Northwestern University graduate student Chuyang Cheng, who won the Distinguished Student Award.
I have featured Buehler’s work here a number of times. The most recent appearance was in a May 29, 2015 posting about synthesizing spider’s silk.
Usually, when science talk runs to spider webs the focus is on strength but this research from the UK and France is all about resilience. From a May 16, 2016 news item on phys.org,
Why doesn’t a spider’s web sag in the wind or catapult flies back out like a trampoline? The answer, according to new research by an international team of scientists, lies in the physics behind a ‘hybrid’ material produced by spiders for their webs.
Pulling on a sticky thread in a garden spider’s orb web and letting it snap back reveals that the thread never sags but always stays taut—even when stretched to many times its original length. This is because any loose thread is immediately spooled inside the tiny droplets of watery glue that coat and surround the core gossamer fibres of the web’s capture spiral.
This phenomenon is described in the journal PNAS by scientists from the University of Oxford, UK and the Université Pierre et Marie Curie, Paris, France.
The researchers studied the details of this ‘liquid wire’ technique in spiders’ webs and used it to create composite fibres in the laboratory which, just like the spider’s capture silk, extend like a solid and compress like a liquid. These novel insights may lead to new bio-inspired technology.
Professor Fritz Vollrath of the Oxford Silk Group in the Department of Zoology at Oxford University said: ‘The thousands of tiny droplets of glue that cover the capture spiral of the spider’s orb web do much more than make the silk sticky and catch the fly. Surprisingly, each drop packs enough punch in its watery skins to reel in loose bits of thread. And this winching behaviour is used to excellent effect to keep the threads tight at all times, as we can all observe and test in the webs in our gardens.’
The novel properties observed and analysed by the scientists rely on a subtle balance between fibre elasticity and droplet surface tension. Importantly, the team was also able to recreate this technique in the laboratory using oil droplets on a plastic filament. And this artificial system behaved just like the spider’s natural winch silk, with spools of filament reeling and unreeling inside the oil droplets as the thread extended and contracted.
Dr Hervé Elettro, the first author and a doctoral researcher at Institut Jean Le Rond D’Alembert, Université Pierre et Marie Curie, Paris, said: ‘Spider silk has been known to be an extraordinary material for around 40 years, but it continues to amaze us. While the web is simply a high-tech trap from the spider’s point of view, its properties have a huge amount to offer the worlds of materials, engineering and medicine.
‘Our bio-inspired hybrid threads could be manufactured from virtually any components. These new insights could lead to a wide range of applications, such as microfabrication of complex structures, reversible micro-motors, or self-tensioned stretchable systems.’
On the heels of my May 29, 2015 post about synthesized spider silk at the Massachusetts Institute of Technology (MIT), researchers at the École Polytechnique de Montréal (Polytechnique Montreal) have also synthesized spider silk according to a June 3, 2015 news item on Nanowerk (Note: A link has been removed),
Professors Frederick Gosselin and Daniel Therriault, along with their master’s student Renaud Passieux, are not related to Spiderman. Nevertheless, these Polytechnique Montreal researchers have produced an ultra-tough polymer fibre directly inspired by spider silk! They recently published an article about the project in the journal Advanced Materials (“Instability-Assisted Direct Writing of Microstructured Fibers Featuring Sacrificial Bonds”).
Three to eight microns in diameter but five to ten times tougher than steel or Kevlar: despite its lightness, spider silk has such remarkable elongation and stretch-resistance properties that humans have long sought to replicate it, in order to make products with those same characteristics.
In large part, spider silk owes its exceptional strength – meaning its ability to absorb a large amount of energy before failing – to the particular molecular structure of the protein chain of which it’s composed. The mechanical origin of its strength drew the interest of researchers at the Laboratory for Multiscale Mechanics in Polytechnique Montréal’s Department of Mechanical Engineering.
“The silk protein coils upon itself like a spring. Each loop of the spring is attached to its neighbours with sacrificial bonds, chemical connections that break before the main molecular structural chain tears,” explained Professor Gosselin, who, along with his colleague Daniel Therriault, is co-supervising Renaud Passieux’s master’s research work. He added: “To break the protein by stretching it, you need to uncoil the spring and break each of the sacrificial bonds one by one, which takes a lot of energy. This is the mechanism we’re seeking to reproduce in laboratory,”
Imitating nature with polymer fibres
Their project involves making micrometric-sized microstructured fibres that have mechanical properties similar to those of spider silk. “It consists in pouring a filament of viscous polymeric solution toward a sub-layer that moves at a certain speed. So we create an instability,” said Renaud Passieux. “The filament forms a series of loops or coils, kind of like when you pour a thread of honey onto a piece of toast. [emphasis mine] Depending on the instability determined by the way the fluid runs, the fibre presents a particular geometry. It forms regular periodic patterns, which we call instability patterns.”
The fibre then solidifies as the solvent evaporates. Some instability patterns feature the formation of sacrificial bonds when the filament makes a loop and bonds to itself. At that point, it takes a pull with a strong energy output on the resulting fibre to succeed in breaking the sacrificial bonds, as they behave like protein-based spider silk.
“This project aims to understand how the instability used in making the substance influences the loops’ geometry and, as a result, the mechanical properties of the fibres we obtain,” explained Professor Therriault. “Our challenge is that the manufacturing process is multiphysical. It draws on concepts from numerous fields: fluid mechanics, microfabrication, strength of materials, polymer rheology and more.”
A vast range of applications for future tough fibre composites
These researchers think that one day, there will certainly be composites obtained by weaving together tough fibres of the type they’re currently developing. Such composites could, for example, make it possible to manufacture new safer and lighter casings for aircraft engines, which would prevent debris from dispersing in case of explosion. Many other applications can be foreseen, from surgical devices to bulletproof clothing to vehicle parts.
Most of the research on spider silk and spider webs that’s featured here is usually from the Massachusetts Institute of Technology (MIT) and, more specifically, from professor Markus J. Buehler. This May 28, 2015 news item on ScienceDaily, which heralds the development of synthetic spider silk, is no exception,
After years of research decoding the complex structure and production of spider silk, researchers have now succeeded in producing samples of this exceptionally strong and resilient material in the laboratory. The new development could lead to a variety of biomedical materials — from sutures to scaffolding for organ replacements — made from synthesized silk with properties specifically tuned for their intended uses.
The findings are published this week in the journal Nature Communications by MIT professor of civil and environmental engineering (CEE) Markus Buehler, postdocs Shangchao Lin and Seunghwa Ryu, and others at MIT, Tufts University, Boston University, and in Germany, Italy, and the U.K.
The research, which involved a combination of simulations and experiments, paves the way for “creating new fibers with improved characteristics” beyond those of natural silk, says Buehler, who is also the department head in CEE. The work, he says, should make it possible to design fibers with specific characteristics of strength, elasticity, and toughness.
The new synthetic fibers’ proteins — the basic building blocks of the material — were created by genetically modifying bacteria to make the proteins normally produced by spiders. These proteins were then extruded through microfluidic channels designed to mimic the effect of an organ, called a spinneret, that spiders use to produce natural silk fibers.
While spider silk has long been recognized as among the strongest known materials, spiders cannot practically be bred to produce harvestable fibers — so this new approach to producing a synthetic, yet spider-like, silk could make such strong and flexible fibers available for biomedical applications. By their nature, spider silks are fully biocompatible and can be used in the body without risk of adverse reactions; they are ultimately simply absorbed by the body.
The researchers’ “spinning” process, in which the constituent proteins dissolved in water are extruded through a tiny opening at a controlled rate, causes the molecules to line up in a way that produces strong fibers. The molecules themselves are a mixture of hydrophobic and hydrophilic compounds, blended so as to naturally align to form fibers much stronger than their constituent parts. “When you spin it, you create very strong bonds in one direction,” Buehler says.
The team found that getting the blend of proteins right was crucial. “We found out that when there was a high proportion of hydrophobic proteins, it would not spin any fibers, it would just make an ugly mass,” says Ryu, who worked on the project as a postdoc at MIT and is now an assistant professor at the Korea Advanced Institute of Science and Technology. “We had to find the right mix” in order to produce strong fibers, he says.
The researchers made use of computational modelling to speed up the process of synthesizing proteins for synthetic spider silk, from the news release,
This project represents the first use of simulations to understand silk production at the molecular level. “Simulation is critical,” Buehler explains: Actually synthesizing a protein can take several months; if that protein doesn’t turn out to have exactly the right properties, the process would have to start all over.
Using simulations makes it possible to “scan through a large range of proteins until we see changes in the fiber stiffness,” and then home in on those compounds, says Lin, who worked on the project as a postdoc at MIT and is now an assistant professor at Florida State University.
Controlling the properties directly could ultimately make it possible to create fibers that are even stronger than natural ones, because engineers can choose characteristics for a particular use. For example, while spiders may need elasticity so their webs can capture insects without breaking, those designing fibers for use as surgical sutures would need more strength and less stretchiness. “Silk doesn’t give us that choice,” Buehler says.
The processing of the material can be done at room temperature using water-based solutions, so scaling up manufacturing should be relatively easy, team members say. So far, the fibers they have made in the lab are not as strong as natural spider silk, but now that the basic process has been established, it should be possible to fine-tune the materials and improve its strength, they say.
“Our goal is to improve the strength, elasticity, and toughness of artificially spun fibers by borrowing bright ideas from nature,” Lin says. This study could inspire the development of new synthetic fibers — or any materials requiring enhanced properties, such as in electrical and thermal transport, in a certain direction.
My two most recent (before this one) postings about Buehler’s work are an August 5, 2014 piece about structural failures and a June 4, 2014 piece about spiderwebs and music.
