Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/92379
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Type: Journal article
Title: Improved synthesis of biotinol-5'-AMP: implications for antibacterial discovery
Author: Tieu, W.
Polyak, S.
Paparella, A.
Yap, M.
Soares Da Costa, T.
Ng, B.
Wang, G.
Lumb, R.
Bell, J.
Turnidge, J.
Wilce, M.
Booker, G.
Abell, A.
Citation: ACS Medicinal Chemistry Letters, 2015; 6(2):216-220
Publisher: American Chemical Society
Issue Date: 2015
ISSN: 1948-5875
1948-5875
Statement of
Responsibility: 
William Tieu, Steven W. Polyak, Ashleigh S. Paparella, Min Y. Yap, Tatiana P. Soares da Costa, Belinda Ng, Geqing Wang, Richard Lumb, Jan M. Bell, John D. Turnidge, Matthew C. J. Wilce, Grant W. Booker, and Andrew D. Abell
Abstract: An improved synthesis of biotinol-5'-AMP, an acyl-AMP mimic of the natural reaction intermediate of biotin protein ligase (BPL), is reported. This compound was shown to be a pan inhibitor of BPLs from a series of clinically important bacteria, particularly Staphylococcus aureus and Mycobacterium tuberculosis, and kinetic analysis revealed it to be competitive against the substrate biotin. Biotinol-5'-AMP also exhibits antibacterial activity against a panel of clinical isolates of S. aureus and M. tuberculosis with MIC values of 1-8 and 0.5-2.5 μg/mL, respectively, while being devoid of cytotoxicity to human HepG2 cells.
Keywords: Antibiotics
enzyme inhibitors
biotin protein ligase
chemical synthesis
drug design
Rights: Copyright © 2014 American Chemical Society
DOI: 10.1021/ml500475n
Grant ID: http://purl.org/au-research/grants/nhmrc/1011806
http://purl.org/au-research/grants/nhmrc/1068885
Published version: http://dx.doi.org/10.1021/ml500475n
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