Abstract
Bacterial type I signal peptidase is a potential target for the development of novel antibacterial agents. In this study we demonstrate that a substrate based peptide aldehyde inhibits signal peptidases with a lower IC(50) value than the lipopeptides described to date. The length of the core lipopeptide could be reduced by removing several amino acids from both termini. Conversion of this peptide to an aldehyde resulted in a molecule with an IC(50) value of 0.09microM when tested against Staphylococcus [corrected] aureus SPase I, SpsB.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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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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Enzyme Inhibitors / chemical synthesis
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Inhibitory Concentration 50
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Membrane Proteins / metabolism*
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Peptides / chemical synthesis
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Peptides / chemistry
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Peptides / pharmacology*
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Saccharomyces / drug effects
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Serine Endopeptidases / metabolism*
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Substrate Specificity
Substances
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Anti-Bacterial Agents
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Enzyme Inhibitors
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Membrane Proteins
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Peptides
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Serine Endopeptidases
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type I signal peptidase