resilin

Resilin is an elastomeric protein found in many arthropods. The protein was first discovered by Torkel Weis-Fogh in the locust wing-hinge. As of 2005 it is the most efficient elastic protein known (Elvin et al., 2005). The elastic efficiency of the resilin isolated from locust tendon has been reported to be 97 % (only 3 % of stored energy is lost as heat). It has no regular structure but its randomly coiled chains are crosslinked by di- and tri-tyrosine links at the right spacing to confer the elasticity needed to propel some jumping insects distances up to 150 times their length (as found in fleas). Resilin must last for the lifetime of adult insects and must therefore operate for hundreds of millions of extension and contraction; its elastic efficiency ensures performance over the insect's lifetime. Resilin exhibits unusual elastomeric behaviour only when swollen in polar solvents such as water.

A multi-disciplinary research team funded by the Australian research body CSIRO published research in Nature on 13 October 2005 on the artificial creation of the protein.

A recombinant form of the vinegar fly resilin protein, pro-resilin, was synthesized in 2005 by expressing a part of the fly gene in the bacterium Escherichia coli. It is expected to have many applications in the athletic footwear, medical, microelectronics and other industries.

References and external links

• CSIRO
• Elvin CM, Carr AG, Huson MG, Maxwell JM, Pearson RD, Vuocolo T, Liyou NE, Wong DC, Merritt DJ, Dixon NE. "Synthesis and properties of crosslinked recombinant pro-resilin" Nature. 2005 Oct 13;437(7061):999-1002 Entrez Pubmed 16222249
• News item from Nature
• Summary from University of South Australia
• Torkel Weis-Fogh: Scientific Papers and Correspondence

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