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

doi:10.1039/C3SC51127H

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

Science and Health

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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.

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 - Sept 2013

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Optimising in situ click chemistry: the screening and identification of biotin protein ligase inhibitors.Accepted author manuscript, 313 KB

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

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

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T1 - Optimising in situ click chemistry

T2 - the screening and identification of biotin protein ligase inhibitors.

AU - Tieu, W.

AU - Soares da Costa, Tatiana

AU - Yap, M.Y.

AU - Keeling, K.L

AU - Wilce, M.C.J.

AU - Wallace, J.C.

AU - Booker, G.W.

AU - Polyak, S.W.

AU - Abell, A.D

N1 - Includes bibliographical references

PY - 2013/9

Y1 - 2013/9

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.

KW - Open access version available

U2 - 10.1039/C3SC51127H

DO - 10.1039/C3SC51127H

M3 - Article

SN - 2041-6520

VL - 4

SP - 3533

EP - 3537

JO - Chemical Science

JF - Chemical Science

IS - 9

ER -

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

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