Abstract
Macrocyclic peptidyl hydroxamates were designed, synthesized, and evaluated as peptide deformylase (PDF) inhibitors. The most potent compound exhibited tight, slow-binding inhibition of Escherichia coli PDF (K(I)(*)=4.4 nM) and had potent antibacterial activity against Gram-positive bacterium Bacillus subtilis (MIC=2-4 microg/mL).
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Amidohydrolases / antagonists & inhibitors*
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Amidohydrolases / chemistry
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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 / drug effects*
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Binding, Competitive / drug effects
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Caproates / chemistry
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Drug Design*
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Hydroxamic Acids / chemical synthesis*
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Hydroxamic Acids / chemistry
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Hydroxamic Acids / pharmacology
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Microbial Sensitivity Tests
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Molecular Structure
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Peptides, Cyclic / chemical synthesis*
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Peptides, Cyclic / chemistry
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Peptides, Cyclic / pharmacology
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Structure-Activity Relationship
Substances
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Anti-Bacterial Agents
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Caproates
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Hydroxamic Acids
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Peptides, Cyclic
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Amidohydrolases
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peptide deformylase