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

William Tieu; Tatiana P Soares da Costa; Min Yin Yap; Kelly L Keeling; Matthew Charles James Wilce; John Campbell Wallace; Grant William Booker; Steven W Polyak; A D Abell

doi:10.1039/C3SC51127H

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

William Tieu, Tatiana P Soares da Costa, Min Yin Yap, Kelly L Keeling, Matthew Charles James Wilce, John Campbell Wallace, Grant William Booker, Steven W Polyak, A D Abell

School of Biomedical Sciences

Research output: Contribution to journal › Article › Research › peer-review

33 Citations (Scopus)

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 language	English
Pages (from-to)	3533 - 3537
Number of pages	5
Journal	Chemical Science
Volume	4
Issue number	9
DOIs	https://doi.org/10.1039/C3SC51127H
Publication status	Published - 2013

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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.",

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AU - Tieu, William

AU - Soares da Costa, Tatiana P

AU - Yap, Min Yin

AU - Keeling, Kelly L

AU - Wilce, Matthew Charles James

AU - Wallace, John Campbell

AU - Booker, Grant William

AU - Polyak, Steven W

AU - Abell, A D

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

UR - http://pubs.rsc.org/en/content/articlelanding/2013/sc/c3sc51127h#!divAbstract

U2 - 10.1039/C3SC51127H

DO - 10.1039/C3SC51127H

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EP - 3537

JO - Chemical Science

JF - Chemical Science

SN - 2041-6539

IS - 9

ER -

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

Abstract

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