Spider silk is the toughest known biomaterial and even outrivals modern synthetic high-performance materials. The question of understanding fiber formation is how the spider can prevent premature and fatal aggregation processes inside its own body and how the chemical and mechanical stimuli used to induce the fiber formation process translate into structural changes of the silk material, finally leading to controlled and irreversible aggregation. Here, the focus will be on the structure and function of the highly conserved N-domains and C-terminal domains of spider dragline silk which, unlike the very long repetitive sequence elements, adopt a folded conformation in solution and are therefore able to control intermolecular interactions and aggregation between other spider silk molecules. The structures of these domains add valuable details for the construction of a molecular picture of the complicated and highly optimized silk assembly process that might be beneficial for large-scale in vitro fiber formation attempts with recombinant silk material.
Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.