The evolutionary origin of modern viscid silk orb webs from ancient cribellate silk ancestors is associated with a 95% increase in diversity of orb-weaving spiders, and their dominance as predators of flying insects, yet the transition's mechanistic basis is an evolutionary puzzle. Ancient cribellate silk is a dry adhesive that functions through van der Waals interactions. Viscid threads adhere more effectively than cribellate threads because of the high extensibility of their axial silk fibers, recruitment of multiple glue droplets, and firm adhesion of the viscid glue droplets. Viscid silk's extensibility is permitted by the glue's high water content, so that organic and inorganic salts present in viscid glue droplets play an essential role in contributing to adhesion by sequestering the atmospheric water that plasticizes the axial silk fibers. Here, we provide direct molecular and macro-scale evidence to show that salts also cause adhesion by directly solvating the glycoproteins, regardless of water content, thus imparting viscoelasticity and allowing the glue droplets to establish good contact. This "dual role" of salts, plasticizing the axial silk indirectly through water sequestration and directly solvating the glycoproteins, provides a crucial link to the evolutionary transition from cribellate silk to viscid silk. In addition, salts also provide a simple mechanism for adhering even at the extremes of relative humidity, a feat eluding most synthetic adhesives.

In addition to DOPA, several other residues including lysine, tryptophan, histidine, arginine and phosphorylated serine are proposed to play key roles in adhesion of mussels and other underwater organisms. [5] In preparing synthetic mimics of mussel adhesives, incorporating DOPA or other hydrophilic moieties is a common theme with the aim that such moieties can potentially outcompete interactions of water with the surface. [6] Interestingly, the role of hydrophobic groups to drive water away has not been exploited in designing underwater adhesives. [7] The adhesive forces required to separate two hydrophobic surfaces apart in water are much higher than the adhesive forces reported for mussel foot proteins on model mica surfaces [8] (measured using surface force apparatus). The removal of water between two hydrophobic surfaces is much easier compared to two hydrophilic surfaces due to strongly hydrated water next to hydrophilic surfaces. [9] Therefore design of adhesives which include hydrophobic groups as a key component is likely to improve adhesion in wet environments. However, designing an adhesive solely based on hydrophobic interactions is not feasible because these surfaces are easily fouled by amphiphilic molecules and result in a rapid decrease in adhesion. [10] Here we show strong evidence that incorporation of hydrophobic and mussel-inspired components in the design of underwater adhesives can substantially improve the performance and durability of such synthetic adhesives.Designing underwater adhesives presents a dichotomy of design principles. To enable spreading of the adhesive without the use of any solvent, the molecular weight needs to be relatively low; however, this would decrease the cohesive strength. To improve cohesive strength, the molecular weight of the poly mer needs to be sufficiently high, but this makes the poly mer glue very viscous or even a solid at room temperature. This would necessitate the use of organic solvents for application of the adhesive, which can be toxic for biomedical applications. [11] Here, we present a unique design of synthetic adhesives by using a combination of soybean oil based hydrophobic and DOPA mimicking catechol pendant functional groups. The soybean oil based hydrophobic groups are important for several reasons. First, they help in lowering the glass transition temperature and the adhesive can be applied Recognizing the potential for synthetic adhesives that can function in wet environments, elements of mussel foot proteins such as L-3,4-dihydroxyphenylalanine (DOPA) and phosphoserine have been incorporated into synthetic adhesives. Such adhesives have corroborated the advantage of surface active groups like DOPA, but have not yet demonstrated superior performance in wet or underwater environments, without using organic solvents. What has been conspicuously absent from such designs is the effect of hydrophobic components in the performance of underwater adhesives. Herein it is shown that incorporation of hydrophobic groups in low modulus polyester adh...

Lipid and protein aggregates are one of the fundamental materials of biological systems. Examples include cell membranes, insect cuticle, vertebrate epidermis, feathers, hair and adhesive structures known as ‘setae’ on gecko toes. Until recently gecko setae were assumed to be composed entirely of keratin, but analysis of footprints left behind by geckos walking on surfaces revealed that setae include various kinds of lipids. However, the arrangement and molecular-level behavior of lipids and keratin in the setae is still not known. In the present study we demonstrate, for the first time, the use of Nuclear Magnetic Resonance (NMR) spectroscopy techniques to confirm the presence of lipids and investigate their association with keratin in ‘pristine' sheds, or natural molts of the adhesive toe pad and non-adhesive regions of the skin. Analysis was also carried on the sheds after they were ‘delipidized’ to remove surface lipids. Our results show a distribution of similar lipids in both the skin and toe shed but with different dynamics at a molecular level. The present study can help us understand the gecko system both biologically and for design of synthetic adhesives, but the findings may be relevant to the characteristics of lipid-protein interactions in other biological systems.

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. LMMCs composition and the humidity at which glue viscosity is optimized vary greatly among spider species. These findings suggest that spiders adapt to forage in diverse habitats by "tuning" LMMCs composition or how LMMCs interact with glycoproteins to control water uptake and adhesion. To test these hypotheses, we analyzed the LMMCs for spiders from diverse habitats and performed water uptake studies on intact glue droplets, isolated glue constituents, and synthetic LMMCs. Even though glue droplets showed differences in water uptake among spider species, we found no differences among species in hygroscopicity of natural or synthetic LMMCs mixtures. This demonstrates that LMMCs composition alone is insufficient to explain interspecific differences in water uptake of spider glues and instead support the hypothesis that an interaction between LMMCs and glycoproteins mediate differences in water uptake and adhesion.

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. Within each droplet an adhesive glycoprotein core condenses. The plasticity and axial line extensibility of the glycoproteins are maintained by hygroscopic LMMCs. These compounds cause droplet volume to track changes in humidity and glycoprotein viscosity to vary approximately 1000-fold over the course of a day. Natural selection has tuned the performance of glycoprotein cores to the humidity of a species' foraging environment by altering the composition of its LMMCs. Thus, species from low-humidity habits have more hygroscopic threads than those from humid forests. However, at their respective foraging humidities, these species' glycoproteins have remarkably similar viscosities, ensuring optimal droplet adhesion by balancing glycoprotein adhesion and cohesion. Optimal viscosity is also essential for integrating the adhesion force of multiple droplets. As force is transferred to a thread's support line, extending droplets draw it into a parabolic configuration, implementing a suspension bridge mechanism that sums the adhesive force generated over the thread span. Thus, viscous capture threads extend an orb spider's phenotype as a highly integrated complex of large proteins and small molecules that function as a self-assembling, highly tuned, environmentally responsive, adhesive biomaterial. Understanding the synergistic role of chemistry and design in spider adhesives, particularly the ability to stick in wet conditions, provides insight in designing synthetic adhesives for biomedical applications.