Abstract
Constitutive proteolytic activity of MALT1 is associated with highly aggressive B-cell lymphomas. Chemical tools that detect active MALT1 have been reported, but suffer from poor cell permeability and/or cross-reactivity with the cysteine protease cathepsin B. Here, we report that the non-natural amino acid pipecolinic acid in the P2 position of substrates and chemical probes leads to improved selectivity toward MALT1 and results in cell-permeable fluorescent probes.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acids / chemical synthesis*
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Amino Acids / metabolism*
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Amino Acids / pharmacology
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Cell Line, Tumor
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Cell Membrane Permeability / drug effects*
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Cell Membrane Permeability / physiology
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Drug Design
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Fluorescent Dyes / chemical synthesis*
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Fluorescent Dyes / metabolism*
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Fluorescent Dyes / pharmacology
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Humans
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Jurkat Cells
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Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein / metabolism*
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Protein Structure, Secondary
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Protein Structure, Tertiary
Substances
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Amino Acids
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Fluorescent Dyes
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MALT1 protein, human
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Mucosa-Associated Lymphoid Tissue Lymphoma Translocation 1 Protein