Abstract
The interaction of a moenomycin derivative with the enzyme penicillin binding protein 1b (PBP 1b) has been studied by means of STD NMR. The results obtained initiated the synthesis of a number of moenomycin derivatives modified in unit A including a moenomycin-ampicillin conjugate and determination of their antibiotic activities. A protocol is described that allows studying the interaction of moenomycin analogues with PBP 1b by fluorescence correlation spectroscopy.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anti-Bacterial Agents / chemical synthesis*
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Anti-Bacterial Agents / pharmacology
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Bacterial Proteins / antagonists & inhibitors*
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Bambermycins / chemical synthesis
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Bambermycins / pharmacology*
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Carrier Proteins / antagonists & inhibitors*
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Diffusion
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Hexosyltransferases / antagonists & inhibitors*
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Microbial Sensitivity Tests
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Muramoylpentapeptide Carboxypeptidase / antagonists & inhibitors*
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Nuclear Magnetic Resonance, Biomolecular / methods
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Octoxynol
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Penicillin-Binding Proteins
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Peptidyl Transferases / antagonists & inhibitors*
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Protein Binding
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Spectrometry, Fluorescence
Substances
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Anti-Bacterial Agents
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Bacterial Proteins
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Carrier Proteins
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Penicillin-Binding Proteins
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Bambermycins
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moenomycin A
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Octoxynol
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Peptidyl Transferases
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Hexosyltransferases
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Muramoylpentapeptide Carboxypeptidase