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Alkylation of staurosporine to derive a kinase probe for fluorescence applications

Disney, Alexander J.M.; Kellam, Barrie; Dekker, Lodewijk V.


Alexander J.M. Disney

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Professor of Medicinal Chemistry


The natural product staurosporine is a high-affinity inhibitor of nearly all mammalian protein kinases.The labelling of staurosporine has proven effective as a means of generating protein kinase research tools. Most tools have been generated by acylation of the 4’-methylamine of the sugar moiety of staurosporine. Herein we describe the alkylation of this group as a first step to generate a fluorescently labelled staurosporine. Following alkylation, a polyethylene glycol linker was installed, allowing subsequent attachment of fluorescein. We report that this fluorescein–staurosporine conjugate binds to cAMP-dependent protein kinase in the nanomolar range. Furthermore, its binding can be antagonised with unmodified staurosporine as well as ATP, indicating it targets the ATP binding site in a similar fashion to native staurosporine. This reagent has potential application as a screening tool for protein kinases of interest.


Disney, A. J., Kellam, B., & Dekker, L. V. (in press). Alkylation of staurosporine to derive a kinase probe for fluorescence applications. ChemMedChem, 11,

Journal Article Type Article
Acceptance Date Feb 10, 2016
Online Publication Date Mar 23, 2016
Deposit Date Feb 27, 2017
Publicly Available Date Feb 27, 2017
Journal ChemMedChem
Print ISSN 1860-7179
Electronic ISSN 1860-7187
Publisher Wiley
Peer Reviewed Peer Reviewed
Volume 11
Public URL
Publisher URL


Disney_et_al-2016-ChemMedChem.pdf (963 Kb)

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