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Self-assembling protein nanofibrils are promising structures for the "bottom-up" fabrication of bionanomaterials. Here, the recombinant protein eADF4(C16), a variant of Araneus diadematus dragline silk ADF4, which self-assembles into nanofibrils, and short oligonucleotides were modified for site-specific azide-alkyne coupling. Corresponding oligonuleotide-eADF4(C16) "click" conjugates were hybridized in linear or branched fashion according to the designed complementarities of the DNA moieties. Self-assembly properties of higher ordered structures of the spider silk-DNA conjugates were dominated by the silk component. Assembled β-sheet rich conjugate fibrils were similar in appearance to fibrils of unmodified eADF4(C16) but enabled the specific attachment of neutravidin-modified gold nanoparticles on their surface directed by complementary biotin-oligonucleotides, providing the basis for functionalization of such conjugates.

Nature has evolved a range of materials that compete with man-made materials in physical properties; one of these is spider silk. Silk is a fibrous material that exhibits extremely high strength and toughness with regard to its low density. In this review we discuss the molecular structure of spider silk and how this understanding has allowed the development of recombinant silk proteins that mimic the properties of natural spider silks. Additionally, we will explore the material morphologies and the applications of these proteins. Finally, we will look at attempts to combine the silk structure with chemical polymers and how the structure of silk has inspired the engineering of novel polymers.

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