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A bifunctional amino acid to study protein–protein interactions

机译:双官能氨基酸研究蛋白质 - 蛋白质相互作用

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Protein–protein interactions (PPIs) play crucial roles in regulating essentially all cellular processes. Photo-cross-linking represents a powerful method to study PPIs. To fulfil the requirements for the exploration of different PPIs, there is a continuous demand on the development of novel photo-reactive amino acids with diverse structural properties and functionalities. Reported herein is the development of a bifunctional amino acid termed dzANA , which contains a diazirine, for photo-cross-linking, and a terminal alkyne group, for bioorthogonal tagging. Using known PPIs between histone posttranslational modifications (PTMs) and their binding partners as models, we demonstrate that the dzANA -harbouring peptide-based photoaffinity probes could efficiently and selectively capture the weak and transient PPIs mediated by histone modifications. Our study indicates the potential of dzANA to identify and characterize unknown PPIs.
机译:蛋白质 - 蛋白质相互作用(PPI)在基本上调节所有细胞过程中起重要作用。光交联表示研究PPI的强大方法。为了满足不同PPI勘探的要求,对具有多种结构性能和功能的新型光反应性氨基酸的开发存在不断的需求。本文报道的是开发含有二氮杂的双官能氨基酸,其用于光交联的二氮杂物和用于生物正交标记的末端炔基。使用已知的PPI在组蛋白后改性(PTMS)和其结合伴侣作为模型之间,我们证明了基于Dzana-karbouring的肽的光遗传探针可以有效地和选择性地捕获由组蛋白修饰介导的弱和瞬时PPI。我们的研究表明Dzana识别和表征未知的PPI的潜力。

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