IspE inhibitors identified by a combination of in silico and in vitro high-throughput screening

Naomi Tidten-Luksch, Raffaella Grimaldi, Leah S. Torrie, Julie A. Frearson, William N. Hunter, Ruth Brenk

    Research output: Contribution to journalArticlepeer-review

    23 Citations (Scopus)

    Abstract

    CDP-ME kinase (IspE) contributes to the non-mevalonate or deoxy-xylulose phosphate (DOXP) pathway for isoprenoid precursor biosynthesis found in many species of bacteria and apicomplexan parasites. IspE has been shown to be essential by genetic methods and since it is absent from humans it constitutes a promising target for antimicrobial drug development. Using in silico screening directed against the substrate binding site and in vitro high-throughput screening directed against both, the substrate and co-factor binding sites, non-substrate-like IspE inhibitors have been discovered and structure-activity relationships were derived. The best inhibitors in each series have high ligand efficiencies and favourable physico-chemical properties rendering them promising starting points for drug discovery. Putative binding modes of the ligands were suggested which are consistent with established structure-activity relationships. The applied screening methods were complementary in discovering hit compounds, and a comparison of both approaches highlights their strengths and weaknesses. It is noteworthy that compounds identified by virtual screening methods provided the controls for the biochemical screens.

    Original languageEnglish
    Article numbere35792
    Pages (from-to)-
    Number of pages16
    JournalPLoS ONE
    Volume7
    Issue number4
    DOIs
    Publication statusPublished - 2012

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