Gumfooted lines in black widow cobwebs and the mechanical properties of spider capture silk.
Orb-weaving spiders produce webs using two types of silk that have radically different mechanical properties. The dragline silk used to construct the supporting frame and radii of the web is stiff and as strong as steel, while the capture spiral is much weaker but more than ten times as extensible. This remarkable divergence in mechanical properties has been attributed to the aqueous glue that coats the capture spiral, which is thought to decrease capture spiral stiffness and increase its extensibility. However, discerning the effect of the aqueous glue on fiber performance is complicated because dragline silk and the capture spiral are assembled from different proteins, which may also affect mechanical performance. Here, we use the sticky gumfooted lines of black widow cobwebs to test the effect of the addition of aqueous glue on the mechanical properties of dragline silk. We also surveyed orb-webs spun by a broad range of species for bundles of looped silk. Such bundles, termed windlasses, have been thought to increase capture spiral extensibility by "paying out" additional lengths of silk. Our results suggest that neither plasticization of silk by aqueous glue nor excess silk in windlasses can by themselves account for the remarkable extensibility of orb-weaver capture silk compared to other spider silks. This argues that the unique amino acid motifs of the flagelliform fibroins that constitute the core of the capture spiral play an essential role in capture silk's extreme extensibility.
Blackledge
Todd A
TA
Department of Biology, University of California, Riverside, CA 92521, USA. tab27@uakron.edu
Summers
Adam P
AP
Hayashi
Cheryl Y
CY
D020816:Amino Acid Motifs / Q000502:physiology; D000818:Animals; D001696:Biomechanical Phenomena; D001740:Black Widow Spider / Q000502:physiology*; D005349:Fibroins / Q000737:chemistry*; D007091:Image Processing, Computer-Assisted; D008859:Microscopy, Polarization / Q000662:veterinary; D047011:Silk / Q000737:chemistry / Q000502:physiology*
D047011:Silk; D005349:Fibroins