MEDI 329 |
| Bacterial enoyl-acyl carrier protein (ACP) reductase is an attractive target for the development of new antibacterial agents. Because it catalyzes the final and an essential step in fatty acid biosynthesis. NADH-dependent reductase, FabI, is widely distributed in bacteria and plants, whereas the enoyl-ACP reductase, FabK, is a distinctly different member of this enzyme group discovered in Streptcoccus pneumoniae. Therefore, an inhibitor of both FabI and FabK is expected to have broad-spectrum antibacterial activities. As a result of SAR studies of FabI and FabK inhibitors from our compound collection, we developed novel 4-pyridone derivatives as strong FabI inhibitor and also developed novel phenylimidazole derivatives as potent FabK inhibitor. From these results and FabK crystal structural study, we assumed that it would be possible to make potent FabI and FabK inhibitors by connecting both 4-pyridone and phenylimidazole moiety. Finally, we found the novel hybrid compounds exhibited potent FabI and FabK inhibitory activities. |
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General Poster Session
7:00 PM-9:00 PM, Wednesday, 13 September 2006 Moscone Center -- Hall D, Poster
Sci-Mix
Division of Medicinal Chemistry |