Chemoenzymatic Synthesis of a MUC1 Glycopeptide Carrying Non-Natural Sialyl TF-.BETA. O-Glycan

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  • TANAKA Eriko
    Department of Applied Biochemistry, Institute of Glycotechnology, Tokai University
  • NAKAHARA Yuko
    Department of Applied Biochemistry, Institute of Glycotechnology, Tokai University
  • KURODA Yasuhiro
    Department of Applied Biochemistry, Institute of Glycotechnology, Tokai University
  • TAKANO Yutaka
    Department of Applied Biochemistry, Institute of Glycotechnology, Tokai University
  • KOJIMA Naoya
    Department of Applied Biochemistry, Institute of Glycotechnology, Tokai University
  • HOJO Hironobu
    Department of Applied Biochemistry, Institute of Glycotechnology, Tokai University
  • NAKAHARA Yoshiaki
    Department of Applied Biochemistry, Institute of Glycotechnology, Tokai University

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Other Title
  • Chemoenzymatic Synthesis of a MUC1 Glycopeptide Carrying Non-Natural Sialyl TF-β O-Glycan
  • Chemoenzymatic Synthesis of a MUC1 Glycopeptide Carrying Non Natural Sialyl TF ベータ O Glycan
  • Chemoenzymatic Synthesis of a MUC1 Glycopeptide Carrying Non-Natural Sialyl TF-β<i>O</i>-Glycan

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Abstract

A MUC1 type of glycopeptide was synthesized by the 9-fluorenylmethoxycarbonyl (Fmoc) solid-phase peptide synthesis (SPPS) protocol using benzyl and benzylidene-protected β-D-Gal-(1→3)-β-D-GalNAc-Ser/Thr (TF-β: a stereoisomer of the Thomsen-Friedenreich antigen). The synthetic glycopeptide was released from the resin with reagent K, and the resulting benzylated glycopeptide was deprotected under conditions of low-acidity trifluoromethanesulfonic acid (TfOH). The glycopeptide carrying duplicate non-natural O-glycans was dominant in the products, but was accompanied by a considerable amount of the glycopeptide missing one of the O-glycans. In contrast, the native α-glycoside was relatively stable under the acidic debenzylation conditions as shown by a parallel experiment with the glycopeptide involving α-D-GalNAc-Ser/Thr linkage. Enzymatic glycosylation with CMP-NeuAc was successful with both natural and non-natural O-glycans of the synthetic glycopeptide.

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