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Issue 11, 2015
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Real-time detection of histone deacetylase activity with a small molecule fluorescent and spectrophotometric probe

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Abstract

Histone deacetylases (HDACs) are central players in transcription regulation and important targets in cancer treatment. Activity assays are critical tools for the study of the function and regulation of these enzymes, as well as for the screening of potential inhibitors. We report a small-molecule probe for single-step, continuous detection of deacetylase activity based on an acetyl-lysine mimic functionalized with an amine-reactive fluorophore, designed to undergo rapid intramolecular imine formation upon deacetylation. The probe exhibits a bathochromic shift in the absorption spectrum and changes in fluorescence emission intensity that enable unprecedented real-time detection of HDAC activity of purified enzymes or in cell lysates, and offers a means to evaluate HDAC inhibitors via simple spectrophotometric or fluorescence readings without the need of additional reagents.

Graphical abstract: Real-time detection of histone deacetylase activity with a small molecule fluorescent and spectrophotometric probe

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Supplementary files

Article information


Submitted
24 Jul 2015
Accepted
30 Jul 2015
First published
03 Aug 2015

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2015,6, 6456-6461
Article type
Edge Article

Real-time detection of histone deacetylase activity with a small molecule fluorescent and spectrophotometric probe

D. R. Rooker and D. Buccella, Chem. Sci., 2015, 6, 6456
DOI: 10.1039/C5SC02704G

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material and it is not used for commercial purposes.

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    [Original citation] - Published by The Royal Society of Chemistry.

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