Work

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

Year: 2013

Type: article

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.

Source: Chemical Science

DOI: 10.1039/c3sc51127h

Authors: 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, Andrew D. Abell

Institutions: The University of Adelaide, Monash University

Language: English

Topic: Click Chemistry and Applications

Subfield: Organic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: green

Funders: Australian Research Council, National Health and Medical Research Council

OpenAlex ID: W2066457093

FWCI: 3.341

Cites: 28

Cited by: 43

Related to: 10