Fluorescence assay to predict activity of the glycopeptide antibiotics
Language English Country Great Britain, England Media print-electronic
Document type Journal Article
PubMed
30504918
DOI
10.1038/s41429-018-0120-5
PII: 10.1038/s41429-018-0120-5
Knihovny.cz E-resources
- MeSH
- Anti-Bacterial Agents metabolism MeSH
- Staining and Labeling MeSH
- Cell Wall microbiology MeSH
- Enterococcus faecium metabolism MeSH
- Vancomycin-Resistant Enterococci metabolism MeSH
- Fluorescence MeSH
- Glycopeptides metabolism MeSH
- Lipoglycopeptides chemistry metabolism MeSH
- Microbial Sensitivity Tests MeSH
- Peptidoglycan metabolism MeSH
- Rhodamines chemistry MeSH
- Staphylococcus aureus metabolism MeSH
- Teicoplanin analogs & derivatives chemistry metabolism MeSH
- Vancomycin chemistry metabolism MeSH
- Protein Binding physiology MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Anti-Bacterial Agents MeSH
- dalbavancin MeSH Browser
- Glycopeptides MeSH
- Lipoglycopeptides MeSH
- oritavancin MeSH Browser
- Peptidoglycan MeSH
- rhodamine isothiocyanate MeSH Browser
- Rhodamines MeSH
- Teicoplanin MeSH
- Vancomycin MeSH
Here, we describe a fluorescent assay developed to study competitive binding of the glycopeptide antibiotics to live bacteria cells. This assay demonstrated that the mechanism of action of the lipoglycopeptide antibiotics strongly depends on the hydrophobicity of the substitutes, with the best antibacterial activity of the glycopeptide antibiotics equally sharing properties of binding to D-Ala-D-Ala residues of the nascent peptidoglycan and to the membrane.
Department of Clinical Medicine UiT The Arctic University of Norway Tromsø Norway
Department of Pediatrics University Hospital of North Norway Tromsø Norway
Department of Pharmaceutical Chemistry University of Debrecen Debrecen Hungary
Institute of Microbiology v v i Czech Academy of Sciences Vestec Czech Republic
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