Abstract
Tunicamycins, which are nucleoside natural products, inhibit both bacterial phospho-N-acetylmuraminic acid (MurNAc)-pentapeptide translocase (MraY) and human UDP-N-acetylglucosamine (GlcNAc): polyprenol phosphate translocase (GPT). The improved synthesis and detailed biological evaluation of an MraY-selective inhibitor, 2, where the GlcNAc moiety was modified to a MurNAc amide, has been described.
Keywords:
antibacterial; nucleoside natural products; organic chemistry.
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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Bacterial Proteins / chemistry
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Cell Line
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Chemistry Techniques, Synthetic
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Humans
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Models, Molecular
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Molecular Conformation
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Molecular Structure
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Structure-Activity Relationship
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Transferases (Other Substituted Phosphate Groups)
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Transferases / antagonists & inhibitors*
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Transferases / chemistry
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Tunicamycin / chemical synthesis*
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Tunicamycin / pharmacology*
Substances
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Anti-Bacterial Agents
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Bacterial Proteins
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Tunicamycin
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Transferases
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Transferases (Other Substituted Phosphate Groups)
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mraY protein, Bacteria