Interactions between Penicillin-Binding Proteins (PBPs) and Two Novel Classes of PBP Inhibitors, Arylalkylidene Rhodanines and Arylalkylidene Iminothiazolidin-4-ones
| Autor: | Wei-Ping Lu, Jean-Marie Frère, Astrid Zervosen, Zhouliang Chen, Thomas P. Demuth, Ronald Eugene White |
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| Rok vydání: | 2004 |
| Předmět: |
Penicillin binding proteins
Rhodanine Stereochemistry Peptidoglycan Alkenes Muramoylpentapeptide Carboxypeptidase medicine.disease_cause Streptomyces Cell wall Structure-Activity Relationship Bacterial Proteins Cell Wall polycyclic compounds Escherichia coli medicine Penicillin-Binding Proteins Structure–activity relationship Protease Inhibitors Pharmacology (medical) Dipeptidyl-Peptidases and Tripeptidyl-Peptidases Mechanisms of Action: Physiological Effects Antibacterial agent Bacillus megaterium Pharmacology Bacteria biology biochemical phenomena metabolism and nutrition biology.organism_classification Kinetics Thiazoles Streptococcus pneumoniae Infectious Diseases Hexosyltransferases Biochemistry Staphylococcus aureus Peptidyl Transferases bacteria Carrier Proteins Algorithms |
| Zdroj: | Antimicrobial Agents and Chemotherapy. 48:961-969 |
| ISSN: | 1098-6596 0066-4804 |
| DOI: | 10.1128/aac.48.3.961-969.2004 |
| Popis: | Several non-β-lactam compounds were active against various gram-positive and gram-negative bacterial strains. The MICs of arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-ones were lower than those of ampicillin and cefotaxime for methicillin-resistant Staphylococcus aureus MI339 and vancomycin-resistant Enterococcus faecium EF12. Several compounds were found to inhibit the cell wall synthesis of S. aureus and the last two steps of peptidoglycan biosynthesis catalyzed by ether-treated cells of Escherichia coli or cell wall membrane preparations of Bacillus megaterium . The effects of the arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-one derivatives on E. coli PBP 3 and PBP 5, Streptococcus pneumoniae PBP 2xS (PBP 2x from a penicillin-sensitive strain) and PBP 2xR (PBP 2x from a penicillin-resistant strain), low-affinity PBP 2a of S. aureus , and the Actinomadura sp. strain R39 and Streptomyces sp. strain R61 dd -peptidases were studied. Some of the compounds exhibited inhibitory activities in the 10 to 100 μM concentration range. The inhibition of PBP 2xS by several of them appeared to be noncompetitive. The dissociation constant for the best inhibitor ( Ki = 10 μM) was not influenced by the presence of the substrate. |
| Databáze: | OpenAIRE |
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