Abstract
New inhibitors of the bacterial transferase MraY are described. Their structure is based on an aminoribosyl-O-uridine like scaffold, readily obtained in two key steps. The amino group can be coupled with proline or guanylated. Alternatively, these amino, prolinyl or guanidinyl groups can be introduced through a triazole linker. Biological evaluation of these compounds on MraY from Bacillus subtilis revealed interesting inhibitory activity for both amino compounds.
Copyright 2010. Published by Elsevier Ltd.
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 / chemistry
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Anti-Bacterial Agents / pharmacology
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Bacillus subtilis / enzymology
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Bacterial Proteins / antagonists & inhibitors*
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Bacterial Proteins / metabolism
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Enzyme Inhibitors / chemical synthesis*
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology
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Transferases (Other Substituted Phosphate Groups)
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Transferases / antagonists & inhibitors*
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Transferases / metabolism
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Triazoles / chemical synthesis
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Triazoles / chemistry
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Triazoles / pharmacology
Substances
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Anti-Bacterial Agents
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Bacterial Proteins
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Enzyme Inhibitors
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Triazoles
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Transferases
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Transferases (Other Substituted Phosphate Groups)
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mraY protein, Bacteria