Abstract
Screening of our compound collection using Staphylococcus aureus Ni–Peptide deformylase (PDF) afforded a very potent PDF inhibitor with an IC 50 in the low nanomolar range but with poor antibacterial activity (MIC). Three-dimensional structural information obtained from Pseudomonas aeruginosa Ni–PDF complexed with the inhibitor suggested the synthesis of a variety of analogues that would maintain high binding affinity while attempting to improve antibacterial activity. Many of the compounds synthesized proved to be excellent PDF–Ni inhibitors and some showed increased antibacterial activity in selected strains.
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