Aequorin is a bioluminescent protein native of the jellyfish Aequorea victoria, capable of emitting light at 469 nm with flash-type kinetics.  Given that bioluminescence is a rare phenomenon in nature, aequorin's bioluminescence can be detected at very low concentrations, which prompt its use in bioanalytical applications.  To enable the use of aequorin in multiple analyte detection, variants of the protein have been created to provide different emission maxima and half-lives.  These variants have been obtained through site-directed and random mutagenesis, incorporation of unnatural amino acids and by pairing the protein with different analogs of the chromophore coelenterazine.  In order to expand the applications of in vitro and in vivo detection using aequorin, we have now dissected (truncated) the protein at different locations to create smaller protein fragments with diverse  bioluminescent properties.  To that end, the characteristics of these new aequorin variants and their potential applications in bioanalysis will be presented.

Dissecting aequorin: From engineering the protein to diversifying its use in bioanalysis

244th National Meeting (2012)

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