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.

中文翻译：

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使用非天然氨基酸设计和合成选择性的，可透过细胞的MALT1活性为基础的探针。

MALT1的组成性蛋白水解活性与高度侵袭性B细胞淋巴瘤相关。已经报道了检测活性MALT1的化学工具，但它们具有差的细胞通透性和/或与半胱氨酸蛋白酶组织蛋白酶B的交叉反应性。在这里，我们报道了底物P2位置的非天然氨基酸哌考林酸和化学试剂探针可提高对MALT1的选择性，并产生可渗透细胞的荧光探针。