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

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

doi:10.1016/S0008-6215(99)00081-6

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

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

School of Medicine

Research output: Contribution to journal › Article › peer-review

29 Scopus citations

Abstract

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 language	English (US)
Pages (from-to)	1-5
Number of pages	5
Journal	Carbohydrate Research
Volume	316
Issue number	1-4
DOIs	https://doi.org/10.1016/S0008-6215(99)00081-6
State	Published - Mar 15 1999

Keywords

Ganglioside GD1α
Myelin-associated glycoprotein
Sialic acid
Sialoadhesins
Siglec

ASJC Scopus subject areas

Analytical Chemistry
Biochemistry
Organic Chemistry

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10.1016/S0008-6215(99)00081-6

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title = "Ganglioside GD1α analogues as high-affinity ligands for myelin-associated glycoprotein (MAG)",

abstract = "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.",

keywords = "Ganglioside GD1α, Myelin-associated glycoprotein, Sialic acid, Sialoadhesins, Siglec",

author = "Naoki Sawada and Hideharu Ishida and Collins, {Brian E.} and Schnaar, {Ronald L.} and Makoto Kiso",

note = "Funding Information: This work was supported by the Ministry of Education, Science and Culture of Japan (grant Nos. 09240101, 10556026 and 10660107). The authors are grateful to Dr Takao Ikami of Sanwa Kagaku Kenkyusho for the FABMS analyses.",

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AU - Sawada, Naoki

AU - Ishida, Hideharu

AU - Collins, Brian E.

AU - Schnaar, Ronald L.

AU - Kiso, Makoto

N1 - Funding Information: This work was supported by the Ministry of Education, Science and Culture of Japan (grant Nos. 09240101, 10556026 and 10660107). The authors are grateful to Dr Takao Ikami of Sanwa Kagaku Kenkyusho for the FABMS analyses.

PY - 1999/3/15

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N2 - 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.

AB - 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.

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KW - Sialoadhesins

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

Abstract

Keywords

ASJC Scopus subject areas

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