Several kinds of natural fibrous proteins have been chosen as models: silk fibroin from Bombyx mori, silks from various species of spiders and collagens. The dragline silk of the spider Nephila clavipes is able to stretch by 30% before breaking and has a high tensile strength. It is stronger per unit weight than high tensile steel. Although the partial sequence of the two components of dragline silk is known, its molecular structure is still far from being clearly established. It is however demonstrated that it contains beta-sheet crystals composed of polyalanine residues. Artificial fibrous proteins have been prepared in vivo using either Escherichia coli or the yeast Pichia pastoris. As these proteins contain repetitive sequences, there is a risk of deletion at the DNA level. This difficulty has been solved by making use of the genetic code degeneracy. One group has successfully synthesized silk-like polymers; prolastin polymers containing both silk-like and elastin-like blocks; proNectin polymers containing the RGD triplet coming from fibronectin and able to fix numerous mammalian cell types; and synthetic collagen analogs. Some of these polymers have been spun into fibers that, up-to-now, do not display any measurable molecular orientation. Another group has studied artificial fibrous proteins able to form beta-sheet crystals of defined thickness and bearing functional groups at their surface, for instance Glu residues, selenomethionine or p-fluorophenylalanine. Apart from university laboratories, a venture capital society, an industrial research center and a US army research center are quite active in this field. A number of parents has been deposited. ((C) Societe francaise de biochimie et biologie moleculaire /Elsevier, Paris).
