Abstract
We explore the chemical space of Pseudomonas quinolone signal analogs as privileged structures and report the discovery of a thioquinolone as a potent inhibitor of the important virulence factor elastase of the human pathogen Pseudomonas aeruginosa. We provide evidence that the derivative binds to the active site zinc of elastase and additionally acts as a fluorescent zinc sensor.
MeSH terms
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Dose-Response Relationship, Drug
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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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Molecular Structure
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Pancreatic Elastase / antagonists & inhibitors*
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Pancreatic Elastase / metabolism
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Pseudomonas aeruginosa / enzymology*
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Quinolones / chemical synthesis
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Quinolones / chemistry
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Quinolones / pharmacology*
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Structure-Activity Relationship
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Virulence Factors / antagonists & inhibitors*
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Virulence Factors / metabolism
Substances
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Enzyme Inhibitors
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Quinolones
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Virulence Factors
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Pancreatic Elastase