Kunz H, Birnbach S, Wernig P
Institut für Organische Chemie, Johannes Gutenberg-Universität Mainz, F.R.G.
Carbohydr Res. 1990 Jul 15;202:207-23. doi: 10.1016/0008-6215(90)84081-5.
Glycopeptides with TN and T antigen structures that represent the N-terminal tripeptide of asialoglycophorin with blood-group M specificity have been synthesized using fluorenylmethoxycarbonyl (Fmoc) and 2-pyridylethoxycarbonyl (Pyoc) groups for amino protection and the benzyl ester as the carboxyl-blocking function. The Fmoc and the Pyoc groups could be removed by treatment with the weak base morpholine under conditions where the base-sensitive O-glycosyl-serine and -threonine linkages were stable. Ester groups were removed from the carbohydrate moieties with methanolic hydrazine, to give the TN and T antigen glycopeptides which were coupled to bovine serum albumin (BSA) via a carbodi-imide procedure and without any spacer groups. The resulting conjugates contained an average of greater than 20 glycopeptides per protein molecule. They are not microheterogeneous in the carbohydrate part as is commonly found for glycoproteins isolated from biological sources.
已使用芴甲氧羰基（Fmoc）和2-吡啶乙氧基羰基（Pyoc）基团进行氨基保护，并以苄酯作为羧基封闭官能团，合成了具有TN和T抗原结构的糖肽，这些结构代表具有血型M特异性的去唾液酸糖蛋白的N端三肽。在碱敏感的O-糖基丝氨酸和苏氨酸键稳定的条件下，用弱碱吗啉处理可除去Fmoc和Pyoc基团。用甲醇肼从碳水化合物部分除去酯基，得到TN和T抗原糖肽，它们通过碳二亚胺程序与牛血清白蛋白（BSA）偶联，且没有任何间隔基团。所得缀合物每个蛋白质分子平均含有超过20个糖肽。它们在碳水化合物部分不存在通常在从生物来源分离的糖蛋白中发现的微观异质性。
