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Bioorg Med Chem Lett. 2004 Mar 22;14(6):1477-81.

Identification of novel potent bicyclic peptide deformylase inhibitors.

Author information

1
Genomics Institute of the Novartis Research Foundation, 10675 John Jay Hopkins Drive, San Diego, CA 92121, USA. vmolteni@gnf.org

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.

PMID:
15006385
DOI:
10.1016/j.bmcl.2004.01.014
[Indexed for MEDLINE]

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