Abstract
A approximately 3500-member library of bidentate inhibitors against protein tyrosine phosphatases (PTPs) was rapidly assembled using click chemistry. Subsequent high-throughput screening had led to the discovery of highly potent (K(i) as low as 150 nM) and selective MptpB inhibitors, some of which represent the most potent MptpB inhibitors developed to date.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / antagonists & inhibitors*
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Drug Discovery*
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Enzyme Inhibitors / analysis*
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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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High-Throughput Screening Assays / methods*
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Molecular Structure
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Protein Tyrosine Phosphatases / antagonists & inhibitors*
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Small Molecule Libraries*
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Stereoisomerism
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Structure-Activity Relationship
Substances
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Bacterial Proteins
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Enzyme Inhibitors
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MptpA protein, Mycobacterium tuberculosis
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Small Molecule Libraries
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Protein Tyrosine Phosphatases