Coumarin inhibitors of gyrase B with N -propargyloxy-carbamate as an effective pyrrole bioisostere
| Autor: | Periers Anne-Marie, Alain Bonnefoy, Didier Ferroud, Michel Klich, Patrice Lassaigne, Pascale Mauvais, Branislav Musicki, Jean-Luc Haesslein, Patrick Laurin, Claudine Dupuis-Hamelin |
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| Rok vydání: | 2000 |
| Předmět: |
Staphylococcus aureus
Isostere Stereochemistry Clinical Biochemistry Pharmaceutical Science Microbial Sensitivity Tests Biochemistry Chemical synthesis DNA gyrase chemistry.chemical_compound Coumarins Drug Discovery Escherichia coli Topoisomerase II Inhibitors Pyrroles heterocyclic compounds Enzyme Inhibitors Molecular Biology Antibacterial agent chemistry.chemical_classification DNA Superhelical Chemistry Organic Chemistry Stereoisomerism Coumarin Anti-Bacterial Agents DNA Gyrase Molecular Medicine Carbamates Bioisostere Antibacterial activity Lactone |
| Zdroj: | Bioorganic & Medicinal Chemistry Letters. 10:161-165 |
| ISSN: | 0960-894X |
| DOI: | 10.1016/s0960-894x(99)00654-x |
| Popis: | The synthesis and biological profile in vitro of a series of coumarin inhibitors of gyrase B bearing a N-propargyloxycarbamate at C-3' of noviose is presented. Replacement of the 5-methylpyrrole-2-carboxylate of coumarin drugs with an N-propargyloxycarbamate bioisostere leads to analogues with improved antibacterial activity. Analysis of crystal structures of coumarin antibiotics with the 24 kDa N-terminal domain of the gyrase B protein provides a rational for the excellent inhibitory potency of C-3' N-alkoxycarbamates. |
| Databáze: | OpenAIRE |
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