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Resilin

From Wikipedia, the free encyclopedia

Resilin is an elastomeric protein found in many arthropods. As of 2005 it is the most efficient elastic protein known. 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 just the right spacing to confer the elasticity needed to propel some jumping insects distances up to 150 times their length. It has been also found that resilin must last for the lifetime of adult insects and must therefore operate for hundreds of millions of cycles of extension and contraction. 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 bacteria Escherichia coli. It is expected to have many applications in the sneaker, medical, micro electronics and other industries.

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