Alkylation of staurosporine to derive a kinase probe for fluorescence applications

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...

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Main Authors: Disney, Alexander J.M., Kellam, Barrie, Dekker, Lodewijk V.
Format: Article
Published: Wiley-VCH Verlag 2016
Online Access:https://eprints.nottingham.ac.uk/40837/
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author Disney, Alexander J.M.
Kellam, Barrie
Dekker, Lodewijk V.
author_facet Disney, Alexander J.M.
Kellam, Barrie
Dekker, Lodewijk V.
author_sort Disney, Alexander J.M.
building Nottingham Research Data Repository
collection Online Access
description 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.
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spelling nottingham-408372020-05-04T17:40:48Z https://eprints.nottingham.ac.uk/40837/ Alkylation of staurosporine to derive a kinase probe for fluorescence applications Disney, Alexander J.M. Kellam, Barrie Dekker, Lodewijk V. 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. Wiley-VCH Verlag 2016-03-23 Article PeerReviewed Disney, Alexander J.M., Kellam, Barrie and Dekker, Lodewijk V. (2016) Alkylation of staurosporine to derive a kinase probe for fluorescence applications. ChemMedChem, 11 . pp. 972-979. ISSN 1860-7187 http://onlinelibrary.wiley.com/doi/10.1002/cmdc.201500589/abstract doi:10.1002/cmdc.201500589 doi:10.1002/cmdc.201500589
spellingShingle Disney, Alexander J.M.
Kellam, Barrie
Dekker, Lodewijk V.
Alkylation of staurosporine to derive a kinase probe for fluorescence applications
title Alkylation of staurosporine to derive a kinase probe for fluorescence applications
title_full Alkylation of staurosporine to derive a kinase probe for fluorescence applications
title_fullStr Alkylation of staurosporine to derive a kinase probe for fluorescence applications
title_full_unstemmed Alkylation of staurosporine to derive a kinase probe for fluorescence applications
title_short Alkylation of staurosporine to derive a kinase probe for fluorescence applications
title_sort alkylation of staurosporine to derive a kinase probe for fluorescence applications
url https://eprints.nottingham.ac.uk/40837/
https://eprints.nottingham.ac.uk/40837/
https://eprints.nottingham.ac.uk/40837/