Sawada N, Ishida H, Collins B E, Schnaar R L, Kiso M
Department of Applied Bio-organic Chemistry, Gifu University, Japan.
Carbohydr Res. 1999 Mar 31;316(1-4):1-5. doi: 10.1016/s0008-6215(99)00081-6.
The first systematic synthesis of ganglioside GD1 alpha 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 GD1 alpha 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.
首次完成了携带与GalNAc残基的C-6相连的N-乙酰脱氧神经氨酸的神经节苷脂GD1α类似物的系统合成。用N-碘代琥珀酰亚胺（NIS）-三氟甲磺酸（TfOH）在乙腈中促进7-脱氧、8-脱氧和9-脱氧-N-乙酰神经氨酸的苯基2-硫代糖苷对适当保护的GM1b五糖衍生物进行区域选择性糖基化，然后将所得六糖转化为目标GD1α类似物。所有类似物在支持与髓鞘相关糖蛋白（MAG）黏附方面均保持优异效率，这增加了与GalNAc残基相连的内部唾液酸可能被其他阴离子取代基取代的可能性，这与对MAG结合至关重要的末端唾液酸形成对比。
