Fluorogenic probe for measuring high-mannose type glycan-specific endo-β-N-acetylglucosaminidase H activity. Issue 13 (1st July 2019)

• Record Type: Journal Article
• Authors: Ishii, Nozomi; Sano, Kanae; Matsuo, Ichiro
• Is Part Of: Bioorganic & medicinal chemistry letters. Volume 29:Issue 13(2019)
• Page Start: 1643
• Page End: 1646
• Publication Date: 2019-07-01
• Subjects: Endo-β-N-acetylglucosaminidase -- Endo-glycosidase -- FRET quenching -- Molecular probe -- Glycosylation; Bioorganic chemistry -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1016/j.bmcl.2019.04.039
• Languages: English
• ISSNs: 0960-894X

Abstract

Graphical abstract: Abstract: We synthesized a fluorogenic probe with a high-mannose type heptasaccharide structure to detect the hydrolytic activity of endo-β- N -acetylglucosaminidase from Streptomyces plicatus (Endo-H). The heptasaccharide derivative (1 ) was labeled with an N -methylanthraniloyl group as a reporter dye at the branching point of the β-mannoside residue and 2, 4-dinitrophenyl group as a quencher molecule at the reducing end, which was hydrolyzed by Endo-H, resulting in increased fluorescence intensity. Thus, Endo-H activities could be evaluated easily and quantitatively by measuring the fluorescence signal. Using both this probe (1 ) and a previously synthesized pentasaccharide probe, the hydrolysis activity of Endo-H and Endo-M were investigated. The results clearly showed a correlation with the substrate specificity of each enzyme.