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Toxicol Lett. 2016 Feb 26;244:161-166. doi: 10.1016/j.toxlet.2015.10.012. Epub 2015 Oct 19.

A novel fluorogenic probe for the investigation of free thiols: Application to kinetic measurements of acetylcholinesterase activity.

Author information

1
Pharmaceutical Institute, Pharmaceutical Chemistry I, University of Bonn, An der Immenburg 4, 53121 Bonn, Germany.
2
Bundeswehr Institute of Pharmacology and Toxicology, Neuherbergstraße 11, 80937 München, Germany.
3
Pharmaceutical Institute, Pharmaceutical Chemistry I, University of Bonn, An der Immenburg 4, 53121 Bonn, Germany; Bundeswehr Institute of Pharmacology and Toxicology, Neuherbergstraße 11, 80937 München, Germany. Electronic address: paul.elsinghorst@uni-bonn.de.

Abstract

A novel coumarin-derived thiol probe, based on the thiol-promoted cleavage of a quenching 2,4-dinitrobenzenesulfonyl group is described. The probe shows a sensitive fluorescence turn-on and sufficient solubility in aqueous environments. As a proof of concept, a new assay for AChE activity was developed as a useful addition to the established Ellman method. The observed reaction kinetics followed an asymmetric sigmoidal pattern and were successfully evaluated applying a three parameter Gompertz equation. Providing a linear relationship between the detected fluorescence formation curves and corresponding enzyme activities, this probe appears as a valuable tool for AChE activity measurements.

KEYWORDS:

Acetylcholinesterase; Activity assay; Fluorescence; Thiols; Turn-on probe

PMID:
26494253
DOI:
10.1016/j.toxlet.2015.10.012
[Indexed for MEDLINE]

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