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      Spider silk fibers spun from soluble recombinant silk produced in mammalian cells.

      Science (New York, N.Y.)
      Amino Acid Motifs, Amino Acid Sequence, Animals, Biopolymers, Birefringence, Cattle, Cell Line, Cloning, Molecular, Cricetinae, Culture Media, Conditioned, DNA, Complementary, Elasticity, Epithelial Cells, metabolism, Fibroins, Materials Testing, Mechanics, Molecular Sequence Data, Molecular Weight, Protein Biosynthesis, Protein Structure, Secondary, Proteins, chemistry, genetics, isolation & purification, Recombinant Proteins, biosynthesis, Solubility, Spiders, Stress, Mechanical, Tensile Strength, Water

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          Abstract

          Spider silks are protein-based "biopolymer" filaments or threads secreted by specialized epithelial cells as concentrated soluble precursors of highly repetitive primary sequences. Spider dragline silk is a flexible, lightweight fiber of extraordinary strength and toughness comparable to that of synthetic high-performance fibers. We sought to "biomimic" the process of spider silk production by expressing in mammalian cells the dragline silk genes (ADF-3/MaSpII and MaSpI) of two spider species. We produced soluble recombinant (rc)-dragline silk proteins with molecular masses of 60 to 140 kilodaltons. We demonstrated the wet spinning of silk monofilaments spun from a concentrated aqueous solution of soluble rc-spider silk protein (ADF-3; 60 kilodaltons) under modest shear and coagulation conditions. The spun fibers were water insoluble with a fine diameter (10 to 40 micrometers) and exhibited toughness and modulus values comparable to those of native dragline silks but with lower tenacity. Dope solutions with rc-silk protein concentrations >20% and postspinning draw were necessary to achieve improved mechanical properties of the spun fibers. Fiber properties correlated with finer fiber diameter and increased birefringence.

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