Fluorescence Polarization Method To Characterize Macrolide-Ribosome Interactions
| Autor: | Robert A. Copeland, Eric Hunt, Earl May, Richard R. Gontarek, Kang Yan, John M. Berge |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
Pharmacology
Analytical Procedures Binding Sites Chemistry Ligand binding assay Erythromycin Fluorescence Polarization medicine.disease_cause Ribosome Anti-Bacterial Agents Dissociation constant Infectious Diseases Biochemistry RNA Ribosomal 23S ribosomal RNA Escherichia coli medicine Pharmacology (medical) Macrolides Binding site Ribosomes Fluorescence anisotropy medicine.drug |
| Zdroj: | Antimicrobial Agents and Chemotherapy. 49:3367-3372 |
| ISSN: | 1098-6596 0066-4804 |
| DOI: | 10.1128/aac.49.8.3367-3372.2005 |
| Popis: | A fluorescence polarization assay is described that measures the binding of fluorescently labeled erythromycin to 70S ribosomes from Escherichia coli and the displacement of the erythromycin from these ribosomes. The assay has been validated with several macrolide derivatives and other known antibiotics. We demonstrate that this assay is suitable for determining the dissociation constants of novel compounds that have binding sites overlapping those of macrolides. This homogeneous binding assay provides a valuable tool for defining structure-activity relationships among compounds during the discovery and development of new ribosome-targeting drugs. |
| Databáze: | OpenAIRE |
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