Issue 9, 2013
From the journal:

Chemical Science

Optimising in situ click chemistry: the screening and identification of biotinprotein ligase inhibitors†

William Tieu,a   Tatiana P. Soares da Costa,b   Min Y. Yap,c   Kelly L. Keeling,a   Matthew C. J. Wilce,c   John C. Wallace,b   Grant W. Booker,b   Steven W. Polyakb  and  Andrew D. Abell*a  

* Corresponding authors

a School of Chemistry and Physics, University of Adelaide, Adelaide, South Australia, Australia
E-mail: andrew.abell@adelaide.edu.au
Fax: +61 8 8303 4358
Tel: +61 0883135652

b School of Molecular and Biomedical Science, University of Adelaide, Adelaide, South Australia, Australia

c School of Biomedical Science, Monash University, Victoria, Australia

Abstract

A ‘leaky mutant’ (SaBPL-R122G) of Staphylococcus aureus biotin protein ligase (SaBPL) is used to enhance the turnover rate for the reaction of biotin alkyne with an azide to give a triazole. This allows the enzyme to select the optimum triazole-based inhibitor using a library of such azides in a single experiment with greatly improved efficiency and sensitivity of detection, difficulties that can restrict the general utility of a multi-component in situ click approach to ligand optimisation.

Graphical abstract: Optimising in situ click chemistry: the screening and identification of biotin protein ligase inhibitors

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Article information

DOI
https://doi.org/10.1039/C3SC51127H
Article type
Edge Article
Submitted
26 Apr 2013
Accepted
19 Jun 2013
First published
19 Jun 2013

Chem. Sci., 2013,4, 3533-3537

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Optimising in situ click chemistry: the screening and identification of biotin protein ligase inhibitors

W. Tieu, T. P. Soares da Costa, M. Y. Yap, K. L. Keeling, M. C. J. Wilce, J. C. Wallace, G. W. Booker, S. W. Polyak and A. D. Abell, Chem. Sci., 2013, 4, 3533 DOI: 10.1039/C3SC51127H

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