Abstract
Protein tyrosine phosphatases (PTPs) have been challenging targets for inhibitor design, because all PTPs share a highly conserved active site structure, which is positively charged and requires negatively charged moieties for tight binding. In this study, we developed cell-permeable bicyclic peptidyl inhibitors against T-cell PTP (TCPTP), which feature a cell-penetrating motif in one ring and a target-binding sequence in the second ring.
MeSH terms
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Combinatorial Chemistry Techniques*
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Dose-Response Relationship, Drug
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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HeLa Cells
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Humans
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Molecular Conformation
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Peptide Library
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Peptides, Cyclic / chemistry
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Peptides, Cyclic / pharmacology*
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Protein Tyrosine Phosphatase, Non-Receptor Type 1 / antagonists & inhibitors*
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Protein Tyrosine Phosphatase, Non-Receptor Type 1 / metabolism
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Protein Tyrosine Phosphatase, Non-Receptor Type 2 / antagonists & inhibitors*
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Protein Tyrosine Phosphatase, Non-Receptor Type 2 / metabolism
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Structure-Activity Relationship
Substances
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Enzyme Inhibitors
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Peptide Library
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Peptides, Cyclic
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PTPN1 protein, human
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Protein Tyrosine Phosphatase, Non-Receptor Type 1
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Protein Tyrosine Phosphatase, Non-Receptor Type 2