Please use this identifier to cite or link to this item:
|Scopus||Web of Science®||Altmetric|
|Title:||Optimising in situ click chemistry: the screening and identification of biotin protein ligase inhibitors|
Soares da Costa, T.
|Citation:||Chemical Science, 2013; 4(9):3533-3537|
|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|
|Appears in Collections:||Aurora harvest 4|
Chemistry and Physics publications
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.