Abstract
A new divalent highly potent inhibitor of the Pseudomonas aeruginosa lectin and virulence factor LecA was prepared. It contains two thiourea linkages which were found to be in the Z,Z isomeric form. This brings the spacer into an elongated conformation required to bridge the two binding sites, which results in the chelating binding mode responsible for the high potency.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adhesins, Bacterial / metabolism*
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Anti-Bacterial Agents / chemistry*
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Anti-Bacterial Agents / pharmacology*
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Humans
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Lectins / antagonists & inhibitors
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Lectins / metabolism
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Molecular Docking Simulation
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Pseudomonas Infections / drug therapy
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Pseudomonas Infections / microbiology
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Pseudomonas aeruginosa / drug effects*
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Pseudomonas aeruginosa / pathogenicity
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Thiourea / analogs & derivatives*
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Thiourea / pharmacology*
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Virulence Factors / antagonists & inhibitors
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Virulence Factors / metabolism*
Substances
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Adhesins, Bacterial
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Anti-Bacterial Agents
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LecA protein, bacteria
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Lectins
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Virulence Factors
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Thiourea