689281-01-4Relevant academic research and scientific papers
Identification of novel potent bicyclic peptide deformylase inhibitors
Molteni, Valentina,He, Xiaohui,Nabakka, Juliet,Yang, Kunyong,Kreusch, Andreas,Gordon, Perry,Bursulaya, Badry,Warner, Ian,Shin, Tanya,Biorac, Tanya,Ryder, Neil S.,Goldberg, Ron,Doughty, John,He, Yun
, p. 1477 - 1481 (2007/10/03)
Screening of our compound collection using Staphylococcus aureus Ni-Peptide deformylase (PDF) afforded a very potent PDF inhibitor with an IC50 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.
