Abstract
High-throughput screening of the P&GP corporate repository against several protein tyrosine phosphatases identified the sulfamic acid moiety as potential phosphotyrosine mimetic. Incorporation of the sulfamic acid onto a 1,2,3,4-tetrahydroisoquinoline scaffold provided a promising starting point for PTP1B inhibitor design.
MeSH terms
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Binding Sites
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Binding, Competitive
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Crystallography, X-Ray
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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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Humans
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Ligands
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Models, Molecular
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Molecular Mimicry
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Phosphotyrosine / metabolism
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Protein Binding
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Protein Tyrosine Phosphatase, Non-Receptor Type 1
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Protein Tyrosine Phosphatases / antagonists & inhibitors*
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Protein Tyrosine Phosphatases / chemistry
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Protein Tyrosine Phosphatases / metabolism
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Structure-Activity Relationship
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Sulfonic Acids / chemical synthesis
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Sulfonic Acids / chemistry
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Sulfonic Acids / pharmacology*
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Tetrahydroisoquinolines / chemistry*
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src Homology Domains
Substances
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Enzyme Inhibitors
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Ligands
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Sulfonic Acids
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Tetrahydroisoquinolines
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Phosphotyrosine
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1,2,3,4-tetrahydroisoquinoline
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sulfamic acid
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PTPN1 protein, human
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Protein Tyrosine Phosphatase, Non-Receptor Type 1
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Protein Tyrosine Phosphatases