Directional web strikes are performed by ray spiders in response to airborne prey vibrations.

Most orb-weaving spiders use static webs that deform only after flying prey hit the webs. However, ray spiders (Theridiosoma gemmosum) pull orb webs into cones that are loaded with enough elastic energy to snap back like slingshots at accelerations of up to 504 m s-2 once released. We test the hypothesis that ray spiders sense vibrations from flying insects to release their webs and capture prey in mid-flight.

Anchor threads can double the insect flight energy absorbed by spider orb webs.

To successfully capture flying insect prey, a spider's orb web must withstand the energy of impact without the silk breaking. In this study, we examined the anchor threads: the silk lines that anchor the main capture area of the web to the surrounding environment. These anchor threads can account for a large portion of the web, yet are usually excluded from experiments and simulations.

Molecular Changes in Spider Viscid Glue As a Function of Relative Humidity Revealed Using Infrared Spectroscopy.

Spider aggregate glue can absorb moisture from the atmosphere to reduce its viscosity and become tacky. The viscosity at which glue adhesion is maximized is remarkably similar across spider species, even though that viscosity is achieved at very different relative humidity (RH) values matching their diverse habitats. However, the molecular changes in the protein structure and the bonding state of water (both referred to here as molecular structure) with respect to the changes in RH are not known.

Permanent deformation of triangle weaver silk enables ultrafast tangle-free release of spider webs.

Entanglements are common in both natural and artificial systems and can result in both beneficial and harmful effects. Most spider webs are static structures held under constant tension and do not tangle. However, many spiders actively load tension into their webs by coiling silk threads that are released to "fire" webs at prey.

Correlation between protein secondary structure and mechanical performance for the ultra-tough dragline silk of Darwin's bark spider.

The spider major ampullate (MA) silk exhibits high tensile strength and extensibility and is typically a blend of MaSp1 and MaSp2 proteins with the latter comprising glycine-proline-glycine-glycine-X repeating motifs that promote extensibility and supercontraction. The MA silk from Darwin's bark spider () is estimated to be two to three times tougher than the MA silk from other spider species. Previous research suggests that a unique MaSp4 protein incorporates proline into a novel glycine-proline-glycine-proline motif and may explain MA silk's extraordinary toughness.

Size-related increase in inducible mechanical variability of major ampullate silk in a huntsman spider (Araneae: Sparassidae).

Most spiders use major ampullate silk (MAS) to perform many functions across their lifetimes, including prey capture, vibratory signal detection, and safety/dragline. To accommodate their various needs, adult spiders can use inducible variability to tailor MAS with specific mechanical properties. However, it is currently unknown whether this inducible mechanical variability develops gradually or remains consistent across spider size.

Robust Performance of Spider Viscid Silk on Hairy and Smooth Insect Substrates.

Spider viscid silk adheres to insects in orb webs and is a "smart-adhesive" that quickly changes droplet size, viscosity, and adhesiveness in response to atmospheric humidity. Different species of spiders "tune" water uptake to match the humidity of their foraging environments, achieving a similar "universal" viscosity that optimizes tradeoffs in spreading versus cohesive bulk energy needed to enhance adhesion. Too much water lowers viscosity so that the glue spreads well, but cohesive failure occurs easily, generating poor adhesion.

Slingshot spiders build tensed, underdamped webs for ultrafast launches and speedy halts.

We develop a mathematical model to capture the web dynamics of slingshot spiders (Araneae: Theridiosomatidae), which utilize a tension line to deform their orb webs into conical springs to hunt flying insects. Slingshot spiders are characterized by their ultrafast launch speeds and accelerations (exceeding 1300 [Formula: see text]), however a theoretical approach to characterize the underlying spatiotemporal web dynamics remains missing. To address this knowledge gap, we develop a 2D-coupled damped oscillator model of the web.

Phylogeny of the orb-weaving spider family Araneidae (Araneae: Araneoidea).

We present a new phylogeny of the spider family Araneidae based on five genes (28S, 18S, COI, H3 and 16S) for 158 taxa, identified and mainly sequenced by us. This includes 25 outgroups and 133 araneid ingroups representing the subfamilies Zygiellinae Simon, 1929, Nephilinae Simon, 1894, and the typical araneids, here informally named the "ARA Clade". The araneid genera analysed here include roughly 90% of all currently named araneid species.

Uncoiling springs promote mechanical functionality of spider cribellate silk.

Composites, both natural and synthetic, achieve novel functionality by combining two or more constituent materials. For example, the earliest adhesive silk in spider webs - cribellate silk - is composed of stiff axial fibers and coiled fibers surrounded by hundreds of sticky cribellate nanofibrils. Yet, little is known of how fiber types interact to enable capture of insect prey with cribellate silk.

The moth specialist spider uses prey scales to increase adhesion.

Contaminants decrease adhesive strength by interfering with substrate contact. Spider webs adhering to moths present an ideal model to investigate how natural adhesives overcome contamination because moths' sacrificial layer of scales rubs off on sticky silk, facilitating escape. However, Cyrtarachninae spiders have evolved gluey capture threads that adhere well to moths.

The transcriptome of Darwin's bark spider silk glands predicts proteins contributing to dragline silk toughness.

Darwin's bark spider () produces giant orb webs from dragline silk that can be twice as tough as other silks, making it the toughest biological material. This extreme toughness comes from increased extensibility relative to other draglines. We show dragline-producing major ampullate (MA) glands highly express a novel silk gene transcript (MaSp4) encoding a protein that diverges markedly from closely related proteins and contains abundant proline, known to confer silk extensibility, in a unique GPGPQ amino acid motif.

Functional trade-offs in cribellate silk mediated by spinning behavior.

Web-building spiders are an extremely diverse predatory group due to their use of physiologically differentiated silk types in webs. Major shifts in silk functional properties are classically attributed to innovations in silk genes and protein expression. Here, we disentangle the effects of spinning behavior on silk performance of the earliest types of capture threads in spider webs for the first time.

Supersaturation with water explains the unusual adhesion of aggregate glue in the webs of the moth-specialist spider, .

Orb webs produced by araneoid spiders depend upon aggregate glue-coated capture threads to retain their prey. Moths are challenging prey for most spiders because their scales detach and contaminate the glue droplets, significantly decreasing adhesion. are moth-specialist orb-weaving spiders whose capture threads adhere well to moths.

Silk structure rather than tensile mechanics explains web performance in the moth-specialized spider, Cyrtarachne.

Orb webs intercept and retain prey so spiders may subdue them. Orb webs are composed of sticky, compliant spirals of capture silk spun across strong, stiff major ampullate silk threads. Interplay between differences in the mechanical properties of these silks is crucial for prey capture.

Role of Hygroscopic Low Molecular Mass Compounds in Humidity Responsive Adhesion of Spider's Capture Silk.

The aggregate glue in spider webs is composed of hygroscopic low molecular mass compounds (LMMCs), glycoproteins and water. The LMMCs absorb atmospheric water and solvate the glycoproteins to spread and adhere to flying insects upon contact. The glue viscosity varies with humidity and there is an optimum range of viscosity where the adhesion is maximum.

Hygroscopic compounds in spider aggregate glue remove interfacial water to maintain adhesion in humid conditions.

Adhesion in humid environments is fundamentally challenging because of the presence of interfacial bound water. Spiders often hunt in wet habitats and overcome this challenge using sticky aggregate glue droplets whose adhesion is resistant to interfacial failure under humid conditions. The mechanism by which spider aggregate glue avoids interfacial failure in humid environments is still unknown.

Tuning orb spider glycoprotein glue performance to habitat humidity.

Orb-weaving spiders use adhesive threads to delay the escape of insects from their webs until the spiders can locate and subdue the insects. These viscous threads are spun as paired flagelliform axial fibers coated by a cylinder of solution derived from the aggregate glands. As low molecular mass compounds (LMMCs) in the aggregate solution attract atmospheric moisture, the enlarging cylinder becomes unstable and divides into droplets.

Rainbow peacock spiders inspire miniature super-iridescent optics.

Colour produced by wavelength-dependent light scattering is a key component of visual communication in nature and acts particularly strongly in visual signalling by structurally-coloured animals during courtship. Two miniature peacock spiders (Maratus robinsoni and M. chrysomelas) court females using tiny structured scales (~ 40 × 10 μm) that reflect the full visual spectrum.

Punctuated evolution of viscid silk in spider orb webs supported by mechanical behavior of wet cribellate silk.

The origin of viscid capture silk in orb webs, from cribellate silk-spinning ancestors, is a key innovation correlated with significant diversification of web-building spiders. Ancestral cribellate silk consists of dry nanofibrils surrounding a stiff, axial fiber that adheres to prey through van der Waals interactions, capillary forces, and physical entanglement. In contrast, viscid silk uses chemically adhesive aqueous glue coated onto a highly compliant and extensible flagelliform core silk.

Spiders have rich pigmentary and structural colour palettes.

Elucidating the mechanisms of colour production in organisms is important for understanding how selection acts upon a variety of behaviours. Spiders provide many spectacular examples of colours used in courtship, predation, defence and thermoregulation, but are thought to lack many types of pigments common in other animals. Ommochromes, bilins and eumelanin have been identified in spiders, but not carotenoids or melanosomes.

Physicochemical Property Variation in Spider Silk: Ecology, Evolution, and Synthetic Production.

The unique combination of great stiffness, strength, and extensibility makes spider major ampullate (MA) silk desirable for various biomimetic and synthetic applications. Intensive research on the genetics, biochemistry, and biomechanics of this material has facilitated a thorough understanding of its properties at various levels. Nevertheless, methods such as cloning, recombination, and electrospinning have not successfully produced materials with properties as impressive as those of spider silk.

Material properties of evolutionary diverse spider silks described by variation in a single structural parameter.

Spider major ampullate gland silks (MAS) vary greatly in material properties among species but, this variation is shown here to be confined to evolutionary shifts along a single universal performance trajectory. This reveals an underlying design principle that is maintained across large changes in both spider ecology and silk chemistry. Persistence of this design principle becomes apparent after the material properties are defined relative to the true alignment parameter, which describes the orientation and stretching of the protein chains in the silk fiber.