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

W. Tieu, Tatiana Soares da Costa, M.Y. Yap, K.L Keeling, M.C.J. Wilce, J.C. Wallace, G.W. Booker, S.W. Polyak, A.D Abell

Research output: Contribution to journalArticle

30 Citations (Scopus)
11 Downloads (Pure)

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.
Original languageEnglish
Pages (from-to)3533-3537
Number of pages5
JournalChemical Science
Volume4
Issue number9
DOIs
Publication statusPublished - Sep 2013

Fingerprint Dive into the research topics of 'Optimising in situ click chemistry: the screening and identification of biotin protein ligase inhibitors.'. Together they form a unique fingerprint.

  • Cite this

    Tieu, W., Soares da Costa, T., Yap, M. Y., Keeling, K. L., Wilce, M. C. J., Wallace, J. C., Booker, G. W., Polyak, S. W., & Abell, A. D. (2013). Optimising in situ click chemistry: the screening and identification of biotin protein ligase inhibitors. Chemical Science, 4(9), 3533-3537. https://doi.org/10.1039/C3SC51127H