Processing and modification of films made from recombinant spider silk proteins

Protein films represent an interesting class of materials with various possibilities for applications. We investigated films made of two different synthetic spider silk proteins derived from the garden spider's (Araneus diadematus) two dragline silk proteins ADF-3 and ADF-4. Protein films cast from hexafluoroisopropanol solutions displayed a predominantly alpha-helical secondary structure. Processing such films with potassium phosphate or methanol resulted in a transition to a beta-sheet rich structure. While as-cast films could be dissolved in water, processed beta-sheet rich films were water insoluble. The chemical stability of processed films depended on the amino acid sequence of the respective protein employed. As a proof of principle, fluorescent probes or enzymes were covalently attached to the film surface. The presented approach provides a basis for designing tailor-made protein films using silk proteins as scaffold, in which the film properties can be controlled by genetic engineering of the underlying silks.