期刊
JOURNAL OF MEDICINAL CHEMISTRY
卷 54, 期 13, 页码 4600-4610出版社
AMER CHEMICAL SOC
DOI: 10.1021/jm2002525
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资金
- EU [LSHM-CT-2004-512138]
- Slovenian Research Agency [P1-0208]
- World Federation of Scientists
MurD ligase is one of the key enzymes participating in the intracellular steps of peptidoglycan biosynthesis and constitutes a viable target in the search for novel antibacterial drugs to combat bacterial drug-resistance. We have designed, synthesized, and evaluated a new series of D-glutamic acid-based Escherichia colt MurD inhibitors incorporating the 5-benzylidenethiazolidin-4-one scaffold. The crystal structure of 16 in the MurD active site has provided a good starting point for the design of structurally optimized inhibitors 73-75 endowed with improved MurD inhibitory potency (IC50 between 3 and 7 mu M). Inhibitors 74 and 75 showed weak activity against Gram-positive Staphylococcus aureus and Enterococcus faecalis. Compounds 73-75, with IC50 values in the low micromolar range, represent the most potent D-Glu-based MurD inhibitors reported to date.
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