Comparison of the spinning of selachian egg case ply sheets and orb web spider dragline filaments.
Liquid crystal spinning appears to be widespread in the animal kingdom, utilizing protein dopes to give materials with a range of different secondary structures including beta-pleat, alpha-helix and collagen-fold. Here we seek to identify the essential design features used in natural liquid crystal spinning by comparing the spinning of two very different materials: the egg case wall of Selachians (dogfish, rays, and their allies) and the dragline silk of orb web spiders. The fish extrudes a "sea and island" composite in which the islands consist of flat ribbons of carefully orientated collagen and the sea, small quantities of an amorphous matrix. Dragline silk filaments are largely constructed from spidroin, a beta protein and have a skin and core structure together with two to three coats. The essential design features common to both systems appear to be the following: (i) intracellular co-storage of a hexagonal columnar liquid crystalline component and a peroxidase within the same secretory vesicles; (ii) luminal storage of a highly concentrated liquid crystalline dope; (iii) use of a dope containing immiscible droplets; (iv) hyperbolic extrusion dies; (v) control of pH and water content of the dope; (vi) preorientation of dope molecules before assembly into fibrils; (vii) combination of extrusion die, treatment/coating bath, and solvent recovery plant within a single microminiaturized device; (viii) slow natural spinning rates. The most important difference is that spiders produce a tough material by unfolding and hydrogen-bonding their silk dope molecules while Selachian fish do it by covalently cross-linking the molecules without unfolding them.
Knight
D P
DP
Department of Zoology, Oxford University, South Parks Road, Oxford OX1 3PS, UK.
Vollrath
F
F
D000818:Animals; D003094:Collagen / Q000096:biosynthesis / Q000737:chemistry* / Q000648:ultrastructure; D004284:Dogfish / Q000033:anatomy & histology / Q000502:physiology*; D019476:Insect Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000648:ultrastructure; D008855:Microscopy, Electron, Scanning; D010063:Ovum / Q000378:metabolism*; D013112:Spiders / Q000033:anatomy & histology / Q000502:physiology*
D019476:Insect Proteins; D003094:Collagen