Spider silk has outstanding mechanical properties despite being spun at close to ambient temperatures and pressures using water as the solvent. The spider achieves this feat of benign fibre processing by judiciously controlling the folding and crystallization of the main protein constituents, and by adding auxiliary compounds, to create a composite material of defined hierarchical structure. Because the 'spinning dope' (the material from which silk is spun) is liquid crystalline, spiders can draw it during extrusion into a hardened fibre using minimal forces. This process involves an unusual internal drawdown within the spider's spinneret that is not seen in industrial fibre processing, followed by a conventional external drawdown after the dope has left the spinneret. Successful copying of the spider's internal processing and precise control over protein folding, combined with knowledge of the gene sequences of its spinning dopes, could permit industrial production of silk-based fibres with unique properties under benign conditions.

Synchrotron FTIR (S-FTIR) microspectroscopy was used to monitor the silk protein conformation in a range of single natural silk fibers (domestic and wild silkworm and spider dragline silk). With the selection of suitable aperture size, we obtained high-resolution S-FTIR spectra capable of semiquantitative analysis of protein secondary structures. For the first time, we have determined from S-FTIR the β-sheet content in a range of natural single silk fibers, 28 ± 4, 23 ± 2, and 17 ± 4% in Bombyx mori, Antheraea pernyi, and Nephila edulis silks, respectively. The trend of β-sheet content in different silk fibers from the current study accords quite well with published data determined by XRD, Raman, and (13)C NMR. Our results indicate that the S-FTIR microspectroscopy method has considerable potential for the study of single natural silk fibers.

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The silk gland of the golden orb spider Nephila edulis connects to the exit spigot through a long S-shaped duct that assists in the formation of the thread. Previous evidence suggests that the epithelium of the distal (last) part of the duct is specialized for ion transport and that a proton pump is involved in this process. Here, we present evidence from SEM (scanning electron microscope)-EDAX (energy dispersive X-ray) microanalysis of rapidly frozen material maintained at approximately -150 degrees C and from the use of pH indicators that the element composition and pH change progressively as the dragline silk dope (spinning solution) passes down the duct to form the thread. Na+ and Cl- composition decreased while K+ and P and S increased. Indicators suggested that the pH dropped from 6.9+/-0.1 to 6.3+/-0.1. These novel findings suggest that the absorption of Na+ and secretion of the more chaotropic K+ may help the silk protein molecules to refold while the secretion of H+ may assist in this process and reduce the repulsive charges on them. This in turn may allow the molecules to approach one another more closely to crystallize. Thus precise control of the ionic environment within the spider's spinning duct may be important in forming a tough insoluble thread and when devising mimetic processes to spin silk proteins industrially.

The rheological properties of fibroin silk solutions extracted from the middle division of Bombyx mori silkworms were examined. Acidification of the solutions with acetic acid vapor gelled the material, a process which at short time scales could be reversed by exposure to ammonia vapor. The solution could also be converted to sol from the gel state by the addition of EDTA. The possible mechanisms for gel formation in fibroin solutions is discussed as are the implications for the process of spinning silk fibers.

Silkworm silk has outstanding mechanical properties despite being spun at room temperature and from aqueous solution. Although it has been proposed that fiber formation is mainly induced by shearing and extensional flow in the spinneret, the detailed structure and function of the spinning apparatus of Bombyx mori silkworms are still not fully elucidated. In this paper we describe three aspects of the functional microanatomy of the spinning apparatus: changes in the diameter of the silk gland duct with distance along the duct, how the birefringence of the fibroin changes as it flows down the duct, and the detailed three-dimensional structure of the silk press and related structures. The existence of a double escaped nematic liquid crystal texture in the fibroin in a region of the duct is described. After this region the birefringence suddenly disappeared until the start of an internal draw down taper which commenced just before the silk press. In the internal draw down taper the birefringence increased dramatically to an asymptotic value as a thread was drawn from the fibroin gel. The structure of the silk press suggests that it acts as a restriction die whose diameter can be regulated.

Our observations on whole mounted major ampullate silk glands suggested that the thread is drawn from a hyperbolic die using a pre-orientated lyotropic liquid crystalline feedstock. Polarizing microscopy of the gland's duct revealed two liquid crystalline optical textures: a curved pattern in the feedstock within the ampulla of the gland and, later in the secretory pathway, the cellular texture previously identi¢ed in synthetic nematic liquid crystals. The behaviour of droplet inclusions within the silk feedstock indicated that elongational £ow at a low shear rate occurs in the gland's duct and may be important in producing an axial molecular orientation before the ¢nal thread is drawn. Our observations suggested that the structure of the spider's silk production pathway and the liquid crystalline feedstock are both involved in de¢ning the exceptional mechanical properties of spider dragline silk.

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