New Series of BPL Inhibitors To Probe the Ribose-Binding Pocket of Staphylococcus aureus Biotin Protein Ligase

Jiage Feng, Ashleigh S. Paparella, William Tieu, David Heim, Sarah Clark, Andrew Hayes, Grant W. Booker, Steven W. Polyak, Andrew D. Abell

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


Replacing the labile adenosinyl-substituted phosphoanhydride of biotinyl-5′-AMP with a N1-benzyl substituted 1,2,3-triazole gave a new truncated series of inhibitors of Staphylococcus aureus biotin protein ligase (SaBPL). The benzyl group presents to the ribose-binding pocket of SaBPL based on in silico docking. Halogenated benzyl derivatives (12t, 12u, 12w, and 12x) proved to be the most potent inhibitors of SaBPL. These derivatives inhibited the growth of S. aureus ATCC49775 and displayed low cytotoxicity against HepG2 cells.

Original languageEnglish
Pages (from-to)1068-1072
Number of pages5
JournalACS Medicinal Chemistry Letters
Issue number12
Publication statusPublished or Issued - 8 Dec 2016
Externally publishedYes


  • Enzyme inhibitors
  • Staphylococcus aureus
  • antibiotics
  • biotin protein ligase

ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry

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