Resilin is a member of a family of elastic proteins that includes elastin, as well as gluten, gliadin, abductin and spider silks. Resilin is found in specialized regions of the cuticle of most insects, providing low stiffness, high strain and efficient energy storage; it is best known for its roles in insect flight and the remarkable jumping ability of fleas and spittle bugs. Previously, the Drosophila melanogaster CG15920 gene was tentatively identified as one encoding a resilin-like protein (pro-resilin). Here we report the cloning and expression of the first exon of the Drosophila CG15920 gene as a soluble protein in Escherichia coli. We show that this recombinant protein can be cast into a rubber-like biomaterial by rapid photochemical crosslinking. This observation validates the role of the putative elastic repeat motif in resilin function. The resilience (recovery after deformation) of crosslinked recombinant resilin was found to exceed that of unfilled synthetic polybutadiene, a high resilience rubber. We believe that our work will greatly facilitate structural investigations into the functional properties of resilin and shed light on more general aspects of the structure of elastomeric proteins. In addition, the ability to rapidly cast samples of this biomaterial may enable its use in situ for both industrial and biomedical applications.

Concerns for the environment and consumer demand are driving research into environmentally friendly fibers as replacements for part of the 38 million tonnes of synthetic fiber produced annually. While much current research focuses on cellulosic fibers, we highlight that protein fibers regenerated from waste or byproduct sources should also be considered. Feather keratin and wheat gluten may both be suitable. They are annually renewable, commercially abundant, of consistent quality, and have guaranteed supply. They contain useful amino acids for fiber making, with interchain cross-linking possible via cysteine residues or through the metal-catalyzed photocrosslinking of tyrosine residues. Previous commercially produced fibers suffered from poor wet strength. Contemporary nanoparticle and cross-linking technology has the potential to overcome this, allowing commercial production to resume. This would bring together two existing large production and processing pipelines, agricultural protein production and textile processing, to divert potential waste streams into useful products.

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