Synthesis of a Versatile Probe for Analysis of Cytoplasmic Peptide-N-Glycanase

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Functions of Peptide-N-Glycanase (PNGase) in endoplasmic reticulum-associated degradation (ERAD) are attracting recent attention. In order to analyze in this process, we developed a potent inhibitor having clickable tag that can allow for a variety of functional groups to be introduced such as detection and purification tags easily using a Cu (I)-catalyzed [3,2] cycloaddition reaction. Our probe inhibited PNGase selectively by micro M order and can easily lead to a variety of compounds. These compounds should help in the understanding of the biological functions of cytoplasmic PNGase.