Synthesis and evaluation of fluorescent probes for the detection of calpain activity
Synthesis and evaluation of fluorescent probes for the detection of calpain activity
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.
calpain i, fret, fluorescence, proteolytic activity
234-238
Mittoo, Stifun
a2ecddb7-743b-4d42-8a59-f3cacc5d68c5
Sundstrom, Lars E.
bb62018d-0157-4274-a865-448ed12934bd
Bradley, Mark
562b9add-34c4-4620-bfa1-c7c83a0f0900
2003
Mittoo, Stifun
a2ecddb7-743b-4d42-8a59-f3cacc5d68c5
Sundstrom, Lars E.
bb62018d-0157-4274-a865-448ed12934bd
Bradley, Mark
562b9add-34c4-4620-bfa1-c7c83a0f0900
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), .
(doi:10.1016/S0003-2697(03)00324-5).
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 ?-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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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
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Date deposited: 28 Apr 2006
Last modified: 15 Mar 2024 07:20
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Author:
Stifun Mittoo
Author:
Lars E. Sundstrom
Author:
Mark Bradley
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