The role of proline in the elastic mechanism of hydrated spider silks.

This study used thermoelastic measurements to investigate the role of proline in the elastic mechanism of hydrated, spider major ampullate (MA) and flagelliform (FL) silks. Experiments on hydrated MA silk from Araneus diadematus (proline content 16%) reveal that conformational entropy elasticity accounts for about 90% of the elastic force at small extensions, but entropy elasticity drops to about half by 50% extension. The decrease in the entropic component with extension is due to the presence of relatively short and conformationally restricted network chains in Araneus MA silk. Experiments on hydrated Araneus FL silk (proline content 16%) indicate that entropy elasticity dominates the elastic mechanism up to extensions of 100% and beyond, which likely reflects the fact that the glycine-rich network chains in FL silk are longer and less conformationally restricted than those in the MA silk. Thus, the rubber-like, entropic elasticity of these two proline-rich silks is consistent with networks of amorphous chains that become mobile when hydrated. By contrast, the elastic mechanism of hydrated Nephila clavipes MA silk (proline content 3.5%) shows a small contribution from entropic elasticity for extensions of 5% or less, and by 10% extension the elastic force is due entirely to bond-energy elasticity, probably associated with the deformation of stable secondary structures. These results indicate that there are major differences in the structural organization of the glycine-rich network chains and the mechanism of elasticity in proline-rich and proline-deficient fibroins.

The effect of proline on the network structure of major ampullate silks as inferred from their mechanical and optical properties.

The silk that orb-weaving spiders produce for use as dragline and for the frame of the web is spun from the major ampullate (MA) glands, and it is renowned for its exceptional toughness. The fibroins that make up MA silk have previously been organized into two major groupings, spidroin-1 and spidroin-2, based largely on differences in amino acid sequence. The most apparent difference between spidroin-1 and spidroin-2 fibroins is the lack of proline in spidroin-1. The MA silk of Araneus diadematus comprises two spidroin-2 fibroins, and is therefore proline-rich, whereas spidroin-1 is preferentially expressed in Nephila clavipes MA silk, and so this silk is proline deficient. Together, these two silks provide a system for testing the consequences of proline-rich and proline-deficient fibroin networks. This study measures the mechanical and optical properties of dry and hydrated Araneus and Nephila MA silks. Since proline acts to disrupt secondary structure, it is hypothesized that the fibroin network of Araneus MA silk will contain less secondary structure than the network of Nephila MA silk. Mechanical and optical studies clearly support this hypothesis. Although the dry properties of these two silks are indistinguishable, there are large differences between the hydrated silks. Nephila silk does not swell upon hydration to the same degree as Araneus silk. In addition, upon hydration, Nephila MA silk retains more of its initial dry stiffness, and retains more molecular order, as indicated by birefringence measurements.

Supercontraction stress in spider webs.

Silk produced from the major ampullate (MA) gland supercontracts when wet, and in this paper, we investigate the consequences of high humidity and of the added load of water droplets condensing from saturated air on the mechanical integrity of the spiders' orb web. We measured the development of the supercontraction stress (sigma(sc)) with time when fixed lengths of MA silk from Nephila clavipes and Argiope aurantia were exposed to increasing humidity. Supercontraction generated stresses of about 50 MPa, and extension of these samples to stresses between 150 and 1100 MPa show a time dependent relaxation over 1000 s to approximately 75% of the initial tension but show no indication of failure. We conclude that supercontraction can maintain tension in webs and does not limit the ability of the web to support loads in excess of the supercontraction stress.