Jump to main content
Jump to site search

Issue 37, 2016
Previous Article Next Article

A direct assay of butyrylcholinesterase activity using a fluorescent substrate

Author affiliations

Abstract

In this study, we report a direct fluorometric assay for butyrylcholinesterase (BChE) activity and screening of its inhibitor, using a fluorescent substrate. 2-(2-(5,6-Dimethoxy-1,3-dioxoisoindolin-2-yl)acetoxy)-N,N,N-trimethylethan-1-ammonium iodide (1) was hydrolyzed by BChE, and its fluorescence was quenched by an intramolecular photoinduced electron transfer process. The resulting change in fluorescence provided a facile method for real-time BChE activity testing. Remarkably, 1 was selectively hydrolyzed by BChE, even in the presence of excess acetylcholinesterase, thereby facilitating the specific monitoring of BChE activity. This assay method is also useful for screening potential BChE inhibitors. Given its simplicity, selectivity, and higher assay speed, this method may be extended to high-throughput screening of BChE inhibitors and relevant drug discovery.

Graphical abstract: A direct assay of butyrylcholinesterase activity using a fluorescent substrate

Back to tab navigation

Supplementary files

Publication details

The article was received on 24 Jun 2016, accepted on 23 Aug 2016 and first published on 24 Aug 2016


Article type: Paper
DOI: 10.1039/C6OB01360K
Org. Biomol. Chem., 2016,14, 8815-8820

  •   Request permissions

    A direct assay of butyrylcholinesterase activity using a fluorescent substrate

    S. Kang, S. Lee, W. Yang, J. Seo and M. S. Han, Org. Biomol. Chem., 2016, 14, 8815
    DOI: 10.1039/C6OB01360K

Search articles by author

Spotlight

Advertisements