NMR identification of ligands of aminoglycoside resistance enzymes

Bacterial resistance to aminoglycosides is mainly the result of enzyme-catalyzed chemical modifications of these antibiotics, which prevents their binding to their target. In order to circumvent this mechanism, an attractive possibility would be to block these enzymes, using selective inhibitors. Th...

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Published inComptes rendus. Chimie Vol. 9; no. 3-4; pp. 413 - 419
Main Authors MAURICE, Frédérique, BEGIS, Guillaume, MICOUIN, Laurent, DARDEL, Frédéric
Format Conference Proceeding Journal Article
LanguageEnglish
French
Published Paris Elsevier 01.03.2006
Académie des sciences (Paris)
Subjects
Biochemistry, Molecular Biology
Biological and medical sciences
Biotechnology
Fundamental and applied biological sciences. Psychology
Health. Pharmaceutical industry
Industrial applications and implications. Economical aspects
Life Sciences
Resistance
Screening
Antibiotic
Enzyme
Ligand
Aminoglycoside
Fluorescence
Enzyme inhibitor
Identification
NMR spectrometry
Nuclear magnetic resonance
antibiotic
screening
flow-injection NMR
fluorescence
deoxystreptamine
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Summary:Bacterial resistance to aminoglycosides is mainly the result of enzyme-catalyzed chemical modifications of these antibiotics, which prevents their binding to their target. In order to circumvent this mechanism, an attractive possibility would be to block these enzymes, using selective inhibitors. This work describes a rational strategy aimed at isolating specific ligands of these enzymes, using NMR spectroscopy. Using magnetization transfer techniques, the identification of contacts between elementary pharmacophores and the protein target allows the guidance of hit improvement from a very early stage.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ISSN:1631-0748
1878-1543
1878-1543
DOI:10.1016/j.crci.2005.06.011