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Using spider silk and collagen as a model, we have investigated the role that various   protein primary structural components play in fibre production. Spidroins, spider dragline   silk protein components, are essentially characterised by an amino-acid repeat containing   a glycine-rich motif (amorphous) followed by an alanine-rich motif (crystalline, putatively   responsible for fibre strength). We have tested the importance of alanine runs in these   proteins and the role of this motif in the mechanical properties of the resulting fibre. To   test the importance of alanine-rich motifs in the spidroin-1 proteins, we engineered three   types of spidroin-1-like genes containing sequence encoding for different amounts of   alanine repeats in the protein (normal, low, and no alanine residues). We also have   engineered three copolymer collagen-spidroin-1 genes using each of the three spidroin-1   synthetic genes. These copolymers were mimicked on the existing natural block collagensilk-   like protein copolymer found in the byssus thread of marine mussels. All of these   constructs were introduced in yeast (Pichia pastoris) for protein production. We are   currently purifying each of the recombinant proteins for structural analysis (CDspectroscopy).

BIOMIMETIC MANUFACTURING OF CUSTOMISED NOVEL FIBRE PROTEINS FOR SPECIALISED APPLICATIONS