Search

Silks produced by silkworms (e.g.,Bombyx mori) and orb-web weaving spiders (e.g.,Nephila clavipes) are essentially pure protein, that is, complexes of amino acid polymers. They are the most common fibers spun by biological systems. There has been a long-standing interest in the use of these and similar fibers in textiles, cables, fiber reinforcement in composites, in addition, for example, to cross hairs in optical instruments, and fishing nets. Both nylon, a homo-polymer of the amino acid glycine, and Kevlar, a polymer of a nonnatural aromatic amino acid, can be considered modified, synthetic versions of silk and are used for some of the applications mentioned above. The potential for genetic manipulation, through recombinant DNA technology, of the natural biosynthetic process for these natural proteins (see the article by Cappello in this issue) has renewed interest in the production of new silklike proteins.The natural silks are characterized by aβ-sheet secondary structure which is stabilized by interchain hydrogen bonds and intersheet hydrophobic interactions (Figure 1). Silks can be considered block copolymers, with crystalline domains consisting of short side chain monomers (the amino acids glycine, alanine, and serine) interspersed in amorphous domains consisting of bulkier side chain amino acids.This family of fibers is naturally tailored to perform functions such as catching prey (orb web) or serving as a barrier against environmental challenges (cocoon). The domestic silkworm (B. mori) produces only one type of silk, cocoon silk, at only one stage in its lifecyle, during the fifth larval instar just before molt to the pupa. The silk is produced in modified salivary glands and spun from the mouth.

NATURAL silk exhibits a strength and stiffness similar to, and a toughness up to ten times greater than, that of artificial high-performance fibres1–5. These exceptional tensile properties, the optical birefringence of some silk secretions6–9 and the molecular order exhibited by some synthetic polypeptides in solution10 all suggest that natural silk secretions might form liquid-crystalline phases. We have now used polarized-light microscopy to study the secretions from major ampullae of spiders (Nephila clavipes) and from silk glands of silkworms (Bombyx mori). As the concentration is increased by evaporation of water, nematic liquid-crystalline microstructures develop. We deduce that natural silk secretions become liquid crystalline after leaving the gland but before solidifying into a fibre, thus promoting global molecular alignment in the fibre. Our hand-drawn fibres from droplets of secretion, as well as sheared thin films, show a banded microstructure which is indicative of a periodic variation in the direction of molecular alignment11. Both B. mori and N. clavipes, on the other hand, have apparently developed processing routes that ensure uniform molecular alignment: the threads and draglines, respectively, of these species do not show banded microstructures.

We have used transmitted polarized light microscopy to examine the fluid contents of silk glands taken from Bombyx mori silkworms and Nephila clavipes orb-weaving spiders. In the absence of shear, the secretions are optically isotropic. As the concentration is allowed to increase by evaporation, microstructures typical of the nematic liquid crystalline state are observed. Thus it appears that naturally spun silk becomes liquid crystalline en route to solidifying into fiber - which is advantageous to introducing and retaining global molecular alignment. This will facilitate the formation of strong, stiff fibers without the need for a significant post-spinning draw. We have also found that natural silk does not exhibit the defects in molecular alignment that are typical of synthetic polymer fibers spun from liquid crystalline solutions or melts.