Wet webs work better: humidity, supercontraction and the performance of spider orb webs.

Like many biomaterials, spider silk responds to water through softening and swelling. Major ampullate silk, the main structural element of most prey capture webs, also shrinks dramatically if unrestrained or develops high tension if restrained, a phenomenon called 'supercontraction'. While supercontraction has been investigated for over 30 years, its consequences for web performance remain controversial. Here, we measured prey capture performance of dry and wet (supercontracted) orb webs of Argiope and Nephila using small wood blocks as prey. Prey capture performance significantly increased at high humidity for Argiope while the improvement was less dramatic for Nephila. This difference is likely due to Argiope silk supercontracting more than Nephila silk. Web deflection, measured as the extension of the web upon prey impact, also increased at high humidity in Argiope, suggesting that silk softening upon supercontraction explains the improved performance of wet webs. These results strongly argue that supercontraction is not detrimental to web performance.

Plasticity in major ampullate silk production in relation to spider phylogeny and ecology.

Spider major ampullate silk is a high-performance biomaterial that has received much attention. However, most studies ignore plasticity in silk properties. A better understanding of silk plasticity could clarify the relative importance of chemical composition versus processing of silk dope for silk properties. It could also provide insight into how control of silk properties relates to spider ecology and silk uses. We compared silk plasticity (defined as variation in the properties of silk spun by a spider under different conditions) between three spider clades in relation to their anatomy and silk biochemistry. We found that silk plasticity exists in RTA clade and orbicularian spiders, two clades that differ in their silk biochemistry. Orbiculariae seem less dependent on external spinning conditions. They probably use a valve in their spinning duct to control friction forces and speed during spinning. Our results suggest that plasticity results from different processing of the silk dope in the spinning duct. Orbicularian spiders seem to display better control of silk properties, perhaps in relation to their more complex spinning duct valve.

Evolution of supercontraction in spider silk: structure-function relationship from tarantulas to orb-weavers.

Spider silk is a promising biomaterial with impressive performance. However, some spider silks also 'supercontract' when exposed to water, shrinking by up to ∼50% in length. Supercontraction may provide a critical mechanism to tailor silk properties, both for future synthetic silk production and by the spiders themselves. Several hypotheses are proposed for the mechanism and function of supercontraction, but they remain largely untested. In particular, supercontraction may result from a rearrangement of the GPGXX motif within the silk proteins, where G represents glycine, P proline and X is one of a small subset of amino acids. Supercontraction may prevent sagging in wet orb-webs or allow spiders to tailor silk properties for different ecological functions. Because both the molecular structures of silk proteins and how dragline is used in webs differ among species, we can test these hypotheses by comparing supercontraction of silk across diverse spider taxa. In this study we measured supercontraction in 28 spider taxa, ranging from tarantulas to orb-weaving spiders. We found that silk from all species supercontracted, except that of most tarantulas. This suggests that supercontraction evolved at least with the origin of the Araneomorphae, over 200 million years ago. We found differences in the pattern of evolution for two components of supercontraction. Stress generated during supercontraction of a restrained fiber is not associated with changes in silk structure and web architecture. By contrast, the shrink of unrestrained supercontracting fibers is higher for Orbiculariae spiders, whose silk contains high ratios of GPGXX motifs. These results support the hypothesis that supercontraction is caused by a rearrangement of GPGXX motifs in silk, and that it functions to tailor silk material properties.

Biomechanical variation of silk links spinning plasticity to spider web function.

Spider silk is renowned for its high tensile strength, extensibility and toughness. However, the variability of these material properties has largely been ignored, especially at the intra-specific level. Yet, this variation could help us understand the function of spider webs. It may also point to the mechanisms used by spiders to control their silk production, which could be exploited to expand the potential range of applications for silk. In this study, we focus on variation of silk properties within different regions of cobwebs spun by the common house spider, Achaearanea tepidariorum. The cobweb is composed of supporting threads that function to maintain the web shape and hold spiders and prey, and of sticky gumfooted threads that adhere to insects during prey capture. Overall, structural properties, especially thread diameter, are more variable than intrinsic material properties, which may reflect past directional selection on certain silk performance. Supporting threads are thicker and able to bear higher loads, both before deforming permanently and before breaking, compared with sticky gumfooted threads. This may facilitate the function of supporting threads through sustained periods of time. In contrast, sticky gumfooted threads are more elastic, which may reduce the forces that prey apply to webs and allow them to contact multiple sticky capture threads. Therefore, our study suggests that spiders actively modify silk material properties during spinning in ways that enhance web function.

How super is supercontraction? Persistent versus cyclic responses to humidity in spider dragline silk.

Spider dragline silk has enormous potential for the development of biomimetic fibers that combine strength and elasticity in low density polymers. These applications necessitate understanding how silk reacts to different environmental conditions. For instance, spider dragline silk ;supercontracts' in high humidity. During supercontraction, unrestrained dragline silk contracts up to 50% of its original length and restrained fibers generate substantial stress. Here we characterize the response of dragline silk to changes in humidity before, during and after supercontraction. Our findings demonstrate that dragline silk exhibits two qualitatively different responses to humidity. First, silk undergoes a previously unknown cyclic relaxation-contraction response to wetting and drying. The direction and magnitude of this cyclic response is identical both before and after supercontraction. By contrast, supercontraction is a ;permanent' tensioning of restrained silk in response to high humidity. Here, water induces stress, rather than relaxation and the uptake of water molecules results in a permanent change in molecular composition of the silk, as demonstrated by thermogravimetric analysis (TGA). Even after drying, silk mass increased by approximately 1% after supercontraction. By contrast, the cyclic response to humidity involves a reversible uptake of water. Dried, post-supercontraction silk also differs mechanically from virgin silk. Post-supercontraction silk exhibits reduced stiffness and stress at yield, as well as changes in dynamic energy storage and dissipation. In addition to advancing understanding supercontraction, our findings open up new applications for synthetic silk analogs. For example, dragline silk emerges as a model for a biomimetic muscle, the contraction of which is precisely controlled by humidity alone.

Supercontraction forces in spider dragline silk depend on hydration rate.

Spider dragline silk is a model biological polymer for biomimetic research due to its many desirable and unusual properties. 'Supercontraction' describes the dramatic shrinking of dragline silk fibers when wetted. In restrained silk fibers, supercontraction generates substantial stresses of 40-50 MPa above a critical humidity of approximately 70% relative humidity (RH). This stress may maintain tension in webs under the weight of rain or dew and could be used in industry for robotics, sensor technology, and other applications. Our own findings indicate that supercontraction can generate stress over a much broader range than previously reported, from 10 to 140 MPa. Here we show that this variation in supercontraction stress depends upon the rate at which the environment reaches the critical level of humidity causing supercontraction. Slow humidity increase, over several minutes, leads to relatively low supercontraction stress, while fast humidity increase, over a few seconds, typically results in higher supercontraction stress. Slowly supercontracted fibers take up less water and differ in thermostability from rapidly supercontracted fibers, as shown by thermogravimetric analysis. This suggests that spider silk achieves different molecular configurations depending upon the speed at which supercontraction occurs. Ultimately, rate-dependent supercontraction may provide a mechanism to tailor the properties of silk or biomimetic fibers for various applications.

The common house spider alters the material and mechanical properties of cobweb silk in response to different prey.

Many spiders depend upon webs to capture prey. Web function results from architecture and mechanical performance of the silk. We hypothesized that the common house spider, Achaearanea tepidariorum, would alter the mechanical performance of its cobweb in response to different prey by varying the structural and material properties of its silk. We fed spiders either large, high kinetic energy crickets or small, low kinetic energy pillbugs for 1 week and then examined their freshly spun silk. We separated mechanical performance into structural and material effects. We measured both types of properties for silk threads collected directly from cobwebs to test for "tuning" of silk performance to different aspects of prey capture. We compared silk from two different functional regions of the cobweb-sticky gumfooted threads that adhere directly to prey and supporting threads that maintain web integrity. Supporting threads from cricket-fed spiders were stiffer and tougher than supporting threads from pillbug-fed spiders. Both types of silk from cricket-fed spiders broke at higher loads than silk from pillbug-fed spiders. We explain this variation using a simple model of forces exerted by prey and spiders on single threads and propose potential mechanisms for this change in material properties. Two alternative, nonexclusive, hypotheses are suggested by our data. Spiders may tune silk to different types of prey by spinning threads that are able to hold prey without deforming permanently. Alternatively, as spider's body mass differed dramatically between the two feeding regimes, spiders may tune silk to their own body mass.

Spider silk aging: initial improvement in a high performance material followed by slow degradation.

Spider silk possesses a unique combination of high tensile strength and elasticity resulting in extraordinarily tough fibers, compared with the best synthetic materials. However, the potential application of spider silk and biomimetic fibers depends upon retention of their high performance under a variety of conditions. Here, we report on changes in the mechanical properties of dragline and capture silk fibers from several spider species over periods up to 4 years of benign aging. We find an improvement in mechanical performance of silk fibers during the first year of aging. Fibers rapidly decrease in diameter, suggesting an increase in structural alignment and organization of molecules. One-year old silk also is stiffer and has higher stress at yield than fresh silk, whereas breaking force, elasticity, and toughness either improve or are unaffected by early aging. However, 4-year old silk shows signs of degradation as the breaking load, elasticity, and toughness are all lower than in fresh silk. Aging, however, does not reduce the tensile strength of silk. These data suggest initially rapid reorganization and tighter packaging of molecules within the fiber, followed by longer-term decomposition. We hypothesize that possibly the breakdown of amino acids via emission of ammonia gas, as is seen in long-term aging of museum silkworm fabrics, may contribute. Degradation of spider silk under benign conditions may be a concern for efforts to construct and utilize biomimetic silk analogs. However, our findings suggest an initial improvement in mechanical performance and that even old spider silk still retains impressive mechanical performance.