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

Record type: Article

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 ?-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.

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Citation

Mittoo, Stifun, Sundstrom, Lars E. and Bradley, Mark (2003) Synthesis and evaluation of fluorescent probes for the detection of calpain activity Analytical Biochemistry, 319, (2), pp. 234-238. (doi:10.1016/S0003-2697(03)00324-5).

More information

Published date: 2003
Keywords: calpain i, fret, fluorescence, proteolytic activity

Identifiers

Local EPrints ID: 27662
URI: http://eprints.soton.ac.uk/id/eprint/27662
ISSN: 0003-2697
PURE UUID: f7ea0a30-c401-4f70-9704-73eef4c0aecb

Catalogue record

Date deposited: 28 Apr 2006
Last modified: 17 Jul 2017 16:04

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Contributors

Author: Stifun Mittoo
Author: Lars E. Sundstrom
Author: Mark Bradley

University divisions

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