Ganglioside GD1α analogues as high-affinity ligands for myelin-associated glycoprotein (MAG)

Naoki Sawada, Hideharu Ishida, Brian E. Collins, Ronald L. Schnaar, Makoto Kiso

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


The first systematic synthesis of ganglioside GD1α analogues carrying N-acetyldeoxyneuraminic acids linked to C-6 of the GalNAc residue was accomplished. The suitably protected GM1b pentasaccharide derivative was regioselectively glycosylated with the phenyl 2-thioglycosides of 7-deoxy, 8-deoxy, and 9-deoxy-N-acetylneuraminic acid promoted by N-iodosuccinimide (NIS)-trifluoromethanesulfonic acid (TfOH) in acetonitrile, and the resulting hexasaccharides were converted to the target GD1α analogues. All of the analogues retained excellent efficiency in supporting the adhesion to myelin-associated glycoprotein (MAG), raising the possibility that the internal sialic acid linked to the GalNAc residue may be replaced by other anionic substituents, in contrast to the terminal sialic acid, which is essential for MAG binding. Copyright (C) 1999 Elsevier Science Ltd.

Original languageEnglish (US)
Pages (from-to)1-5
Number of pages5
JournalCarbohydrate Research
Issue number1-4
StatePublished - Mar 15 1999


  • Ganglioside GD1α
  • Myelin-associated glycoprotein
  • Sialic acid
  • Sialoadhesins
  • Siglec

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry


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