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Fluorescence assay to predict activity of the glycopeptide antibiotics
V. Vimberg, R. Gazak, Z. Szűcs, A. Borbás, P. Herczegh, JP. Cavanagh, L. Zieglerova, J. Závora, V. Adámková, G. Balikova Novotna,
Language English Country Japan
Document type Journal Article
Grant support
NV15-28807A
MZ0
CEP Register
Digital library NLK
Full text - Article
Source
NLK
ProQuest Central
from 2005-01-01 to 1 year ago
Health & Medicine (ProQuest)
from 2005-01-01 to 1 year ago
- 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
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 Pharmaceutical Chemistry University of Debrecen Debrecen Hungary
Institute of Microbiology v v i Czech Academy of Sciences Vestec Czech Republic
References provided by Crossref.org
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- $a 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.
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