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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 ,费时较长的缺点
OBJECTIVE: To study the relationship between the biological structure and biological activity of Glycosylation on HBV Pre S (2), including the location, type, amount and length of sugar chain, and to establish a synthetic peptide other than N or O linked glycosylation Alpha and epsilon amino glycosylation methods. Methods Chemically, mono-, di-, and glycans are covalently attached to the alpha and epsilon amino-containing amino acid residues on the PreS (2) synthetic peptide, specifically the alpha amino group attached to the N-terminus of the peptide and the epsilon of K16 Amino. The two amino acid residues are at or near one of the CTL epitopes recognized on Pre S (2), with amino acid residues 1-15. Results The yields of glycosylation of Mannan, GalNAc and Glc Gal of Pre S (2) were 24.0%, 24.5% and 21.0%, respectively. After the reduction treatment, the stability increased significantly. The HPLC profile shows an inclusion peak. Conclusion The results show that this method has high glycosylation efficiency, which provides a new method for studying the immunological activity of Pre S2 glycopeptide. However, there is a disadvantage that the uniformity of glycosylation is poor and time-consuming