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Anal Biochem. 2003 Aug 15;319(2):234-8.

Synthesis and evaluation of fluorescent probes for the detection of calpain activity.

Author information

1
Department of Chemistry, University of Southampton, Highfield, UK.

Abstract

Two new probes for the detection of calpain I activity based on fluorescence resonance energy transfer technology have been synthesized and evaluated. The probes incorporated the cleavage site present in alpha-spectrin, a naturally occurring substrate of calpain I. The design of the internally quenched substrates is such that the calpain-sensitive bond of the peptides (between the Tyr-Gly residues) is located centrally between the donor and the quencher chromophores. The calpain assay protocol is capable of detecting enzymatic activity in the nanomolar region.

PMID:
12871716
DOI:
10.1016/s0003-2697(03)00324-5
[Indexed for MEDLINE]

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