Work

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

Year: 2016

Type: article

Abstract: 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 ( Sa BPL). The benzyl group presents to the ribose-binding pocket of Sa BPL based on in silico docking. Halogenated benzyl derivatives ( 12t, 12u, 12w, and 12x ) proved to be the most potent inhibitors of Sa BPL. These derivatives inhibited the growth of S. aureus ATCC49775 and displayed low cytotoxicity against HepG2 cells.

Source: ACS Medicinal Chemistry Letters

DOI: 10.1021/acsmedchemlett.6b00248