Binding of monobactams to penicillin-binding proteins of Escherichia coli and Staphylococcus aureus: relation to antibacterial activity
| Autor: | N H Georgopapadakou, C M Cimarusti, S A Smith, Richard B. Sykes |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Staphylococcus aureus
Penicillin binding proteins Cefotaxime Carboxypeptidases Muramoylpentapeptide Carboxypeptidase Biology medicine.disease_cause Microbiology Structure-Activity Relationship Bacterial Proteins Escherichia coli polycyclic compounds medicine Penicillin-Binding Proteins Monobactam Pharmacology (medical) Pharmacology Azlocillin biochemical phenomena metabolism and nutrition Aminoacyltransferases Anti-Bacterial Agents Penicillin Infectious Diseases Hexosyltransferases Biochemistry Peptidyl Transferases bacteria Carrier Proteins Research Article medicine.drug Piperacillin |
| Zdroj: | Antimicrobial Agents and Chemotherapy. 23:98-104 |
| ISSN: | 1098-6596 0066-4804 |
| Popis: | A series of novel monocyclic beta-lactam antibiotics having side chains related to penicillin, piperacillin, azlocillin, and cefotaxime were examined with respect to binding to essential penicillin-binding proteins (PBPs) in Escherichia coli and Staphylococcus aureus. In the penicillin series, there was poor binding to all essential PBPs of E. coli (greater than 100 micrograms/ml) but good binding to PBPs 1, 2, and 3 of S. aureus (approximately 1 microgram/ml). In the piperacillin and azlocillin series, there was good binding to PBP 3 of E. coli (0.1 microgram/ml) and PBPs 1, 2, and 3 of S. aureus (approximately 1 microgram/ml). In the cefotaxime series, there was generally good binding to PBP 3 of E. coli (0.1 micrograms/ml) but poor binding to PBPs 1, 2, and 3 of S. aureus (greater than or equal to 100 micrograms/ml). With a few exceptions in the cefotaxime series, antibacterial activity paralleled essential PBP binding. Binding studies with radioactively labeled compounds revealed no additional essential monobactam-binding proteins in the two organisms. The studies suggest that monobactams are intrinsically active against both gram-positive and gram-negative bacteria; the activity spectrum of a given monobactam is determined by the binding to essential PBPs, which in turn is determined by the nature of the substituents on the beta-lactam nucleus. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|