Improved synthesis of biotinol-5'-AMP: implications for antibacterial discovery

William Tieu; Steven W Polyak; Ashleigh S Paparella; Min Yin Yap; Tatiana P Soares da Costa; Belinda Ng; Geqing Wang; Richard Lumb; Jan M Bell; John D Turnidge; Matthew C Wilce; Grant W Booker; Andrew D Abell

doi:10.1021/ml500475n

Improved synthesis of biotinol-5'-AMP: implications for antibacterial discovery

William Tieu, Steven W Polyak, Ashleigh S Paparella, Min Yin Yap, Tatiana P Soares da Costa, Belinda Ng, Geqing Wang, Richard Lumb, Jan M Bell, John D Turnidge, Matthew C Wilce, Grant W Booker, Andrew D Abell

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

13 Citations (Scopus)

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 mug/mL, respectively, while being devoid of cytotoxicity to human HepG2 cells.

Original language	English
Pages (from-to)	216 - 220
Number of pages	5
Journal	ACS Medicinal Chemistry Letters
Volume	6
Issue number	2
DOIs	https://doi.org/10.1021/ml500475n
Publication status	Published - 2015

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Tieu, William ; Polyak, Steven W ; Paparella, Ashleigh S ; Yap, Min Yin ; Soares da Costa, Tatiana P ; Ng, Belinda ; Wang, Geqing ; Lumb, Richard ; Bell, Jan M ; Turnidge, John D ; Wilce, Matthew C ; Booker, Grant W ; Abell, Andrew D. / Improved synthesis of biotinol-5'-AMP: implications for antibacterial discovery. In: ACS Medicinal Chemistry Letters. 2015 ; Vol. 6, No. 2. pp. 216 - 220.

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title = "Improved synthesis of biotinol-5'-AMP: implications for antibacterial discovery",

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 mug/mL, respectively, while being devoid of cytotoxicity to human HepG2 cells.",

author = "William Tieu and Polyak, {Steven W} and Paparella, {Ashleigh S} and Yap, {Min Yin} and {Soares da Costa}, {Tatiana P} and Belinda Ng and Geqing Wang and Richard Lumb and Bell, {Jan M} and Turnidge, {John D} and Wilce, {Matthew C} and Booker, {Grant W} and Abell, {Andrew D}",

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doi = "10.1021/ml500475n",

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Improved synthesis of biotinol-5'-AMP: implications for antibacterial discovery. / Tieu, William; Polyak, Steven W; Paparella, Ashleigh S; Yap, Min Yin; Soares da Costa, Tatiana P; Ng, Belinda; Wang, Geqing; Lumb, Richard; Bell, Jan M; Turnidge, John D; Wilce, Matthew C; Booker, Grant W; Abell, Andrew D.

In: ACS Medicinal Chemistry Letters, Vol. 6, No. 2, 2015, p. 216 - 220.

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

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AU - Tieu, William

AU - Polyak, Steven W

AU - Paparella, Ashleigh S

AU - Yap, Min Yin

AU - Soares da Costa, Tatiana P

AU - Ng, Belinda

AU - Wang, Geqing

AU - Lumb, Richard

AU - Bell, Jan M

AU - Turnidge, John D

AU - Wilce, Matthew C

AU - Booker, Grant W

AU - Abell, Andrew D

PY - 2015

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AB - 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 mug/mL, respectively, while being devoid of cytotoxicity to human HepG2 cells.

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