摘要
目的 为研究HBVPre S( 2 ) 上糖基化 (Glycosylation)结构差异 (包括位置、种类、数量和糖链长度差异 )与其生物学活性关系 ,建立一种N 或O 连接糖基化以外的合成肽α 和ε 氨基糖基化方法。方法 用化学方法将单、双和聚糖共价连接在Pre S( 2 ) 合成肽上的含α 和ε 氨基的氨基酸残基上 ,即具体连接在肽N端M1的α 氨基和K16的ε 氨基上。此二氨基酸残基位于或接近Pre S( 2 ) 上公认的一个CTL表位 ,氨基酸残基 1～ 15。结果 Pre S( 2 ) 合成肽聚糖 (Mannan)、单糖 (GalNAc)和双糖 (Glc Gal)糖基化的收益率分别为2 4.0 %、2 4.5 %和 2 1.0 %。经还原处理后 ,稳定性显著增加。HPLC图谱显示一包容峰。结论 结果显示此方法具较高的糖基化效率 ,为研究Pre S2 糖肽免疫学活性提供了一种新手段。但存在糖基化的均一性欠佳 。
Objective To design a new method of glycosylation for studying the relationship between the structural heterogeneity of carbohydrates and biological activity of glycoproteins. Methods The Pre S (2) peptides were glycosylated by the covalent binding of carbonyl in open chain form of monosaccharides (or disaccharides, polysaccharides) to α (M1)or ε amino groups (K16) by chemical method, and the residues were situated in or near to the CTL epitope(1～15) of Pre S (2) . Results The yield (%) of mannan, Gal NAc and Glc Gal glycosylated synthetic Pre S (2) in different reaction time were 24.0%, 24.5% and 21.0%. After reducation of C=N to C-N by pyridine borane complexes the stability of glycosylation could be reinforced. Conclusion This method possesses a high efficiency of glycosylation, but with some shortcomings such as time consuming and the homogeneity of glycosylation is not good enough.
出处
《第三军医大学学报》
CAS
CSCD
北大核心
2000年第10期965-968,共4页
Journal of Third Military Medical University
基金
国家自然科学基金资助项目 !(397890 1 0 )
