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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,
Jazyk angličtina Země Japonsko
Typ dokumentu časopisecké články
Grantová podpora
NV15-28807A
MZ0
CEP - Centrální evidence projektů
Digitální knihovna NLK
Plný text - Článek
Zdroj
NLK
ProQuest Central
od 2005-01-01 do Před 1 rokem
Health & Medicine (ProQuest)
od 2005-01-01 do Před 1 rokem
- MeSH
- antibakteriální látky metabolismus MeSH
- barvení a značení MeSH
- buněčná stěna mikrobiologie MeSH
- Enterococcus faecium metabolismus MeSH
- enterokoky rezistentní vůči vankomycinu metabolismus MeSH
- fluorescence MeSH
- glykopeptidy metabolismus MeSH
- lipoglykopeptidy chemie metabolismus MeSH
- mikrobiální testy citlivosti MeSH
- peptidoglykan metabolismus MeSH
- rhodaminy chemie MeSH
- Staphylococcus aureus metabolismus MeSH
- teikoplanin analogy a deriváty chemie metabolismus MeSH
- vankomycin chemie metabolismus MeSH
- vazba proteinů fyziologie MeSH
- Publikační typ
- časopisecké články 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
Citace poskytuje Crossref.org
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