Abstract
We report the first synthesis of a 5S penem, known to bind bacterial type I signal peptidase, from the commercially available and inexpensive 6-aminopenicillanic acid. We report the first in vivo activity of the compound and use structure-activity relationship studies to begin to define the determinants of signal peptidase binding and also to begin to optimize the penem as an antibiotic.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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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Membrane Proteins / antagonists & inhibitors*
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Membrane Proteins / metabolism
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Microbial Sensitivity Tests
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Penicillanic Acid / analogs & derivatives*
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Penicillanic Acid / chemical synthesis
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Penicillanic Acid / chemistry
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Penicillanic Acid / pharmacology
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Serine Endopeptidases / metabolism
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Serine Proteinase Inhibitors / chemical synthesis*
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Serine Proteinase Inhibitors / chemistry
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Serine Proteinase Inhibitors / pharmacology
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Structure-Activity Relationship
Substances
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Anti-Bacterial Agents
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Membrane Proteins
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Serine Proteinase Inhibitors
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Penicillanic Acid
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Serine Endopeptidases
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type I signal peptidase
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aminopenicillanic acid