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Sialyl Tn Unit with TFA‐Labile Protection Realizes Efficient Synthesis of Sialyl Glycoprotein
Author(s) -
Takeda Naoki,
Takei Toshiki,
Asahina Yuya,
Hojo Hironobu
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201706127
Subject(s) - trifluoroacetic acid , chemistry , glycopeptide , sialic acid , glycan , thioester , peptide , combinatorial chemistry , muc1 , peptide synthesis , tandem , glycoprotein , biochemistry , mucin , organic chemistry , enzyme , materials science , composite material , antibiotics
Amino acids bearing 4‐methylbenzyl (MBn) and 4‐methoxybenzyl (MPM)‐protected sialic acid were synthesized and used for the 9‐fluorenylmethoxycarbonyl (Fmoc) solid‐phase synthesis of a glycopeptide. The α‐sialyl linkage of the MBn‐protected unit was partially cleaved under the final deprotection by trifluoroacetic acid (TFA). In addition, the removal of several MBn groups were incomplete. On the other hand, the MPM‐protected unit gave the desired glycopeptide without decomposition of the α‐sialyl linkage. Using this unit, peptide thioesters of the tandem repeat unit of MUC1 mucin were synthesized by the N ‐alkylcysteine (NAC) method and used for the one‐pot ligation by the thioester method. As a result, the three tandem repeats of MUC1 carrying sialyl Tn antigens were successfully synthesized.