Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/80639
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Type: Journal article
Title: Optimising in situ click chemistry: the screening and identification of biotin protein ligase inhibitors
Author: Tieu, W.
Soares da Costa, T.
Yap, M.
Keeling, K.
Wilce, M.
Wallace, J.
Booker, G.
Polyak, S.
Abell, A.
Citation: Chemical Science, 2013; 4(9):3533-3537
Publisher: RSC Publications
Issue Date: 2013
ISSN: 2041-6520
2041-6539
Statement of
Responsibility: 
William Tieu, Tatiana P. Soares da Costa, Min Y. Yap, Kelly L. Keeling, Matthew C. J. Wilce, John C. Wallace, Grant W. Booker, Steven W. Polyak and Andrew D. Abell
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. © 2013 The Royal Society of Chemistry.
Rights: © Royal Society of Chemistry 2013
DOI: 10.1039/c3sc51127h
Appears in Collections:Aurora harvest 4
Chemistry and Physics publications

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