Resilin

Beating of the maxillipeds of the crayfish Pacifastacus leniusculus captured at a frame rate of 1000 s-1

CSIRO Image of a flea with detail showing the resilin pad

Resilin is an elastomeric protein found in many insects. It is part of what enables insects of many species to jump or pivot their wings efficiently. It was first discovered by Torkel Weis-Fogh in locust wing-hinges.

Resilin is currently 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 does not have any 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 38 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 extensions and contractions; its elastic efficiency ensures performance during the insect's lifetime. Resilin exhibits unusual elastomeric behaviour only when swollen in polar solvents such as water.

A recombinant form of the resilin protein of the fly Drosophila melanogaster, 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

• Summary from University of South Australia
• Torkel Weis-Fogh: Scientific Papers and Correspondence