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乙肝表面抗原-CD40L胞外段融合蛋白的设计和生物活性预测
引用本文:林贤凡,吴金明,陈瑾,孙慧,申苏建,金思思. 乙肝表面抗原-CD40L胞外段融合蛋白的设计和生物活性预测[J]. 温州医学院学报, 2009, 39(3): 205-208
作者姓名:林贤凡  吴金明  陈瑾  孙慧  申苏建  金思思
作者单位:温州医学院附属第一医院,消化内科,浙江,温州,325000
摘    要:目的:探讨乙肝表面抗原-CD40L胞外段融合蛋白设计的合理性。方法:应用Gene Constructionkit2.5、DNAStar软件和WWW.expasy.org网站提供的分析方案分析重组体的开放读框以及融合蛋白的柔性、亲水性、抗原性、表位等性质,并作了二级结构模拟分析。结果:重组体CMV启动子下游有完整的目的基因ORF,融合蛋白二级结构水平未出现新的抗原性及表位,亲水性无改变,Linker部位抗原性低,呈中性且柔性高,不影响两端的蛋白质二级结构及融合蛋白空间构象。结论:重组体设计合理,融合蛋白很大可能保留了乙肝表面抗原和CD40L胞外段的生物学活性,为进一步研究提供了理论依据。

关 键 词:乙型肝炎病毒表面抗原  CD40配体  分子结构预测

Design of HBsAg-ecdCD40L fusion protein and prediction of its biological characteristics
LIN Xian-fan,WU Jin-ming,CHEN Jin,SUN Hui,SHEN Su-jian,JIN Si-si. Design of HBsAg-ecdCD40L fusion protein and prediction of its biological characteristics[J]. Journal of Wenzhou Medical College, 2009, 39(3): 205-208
Authors:LIN Xian-fan  WU Jin-ming  CHEN Jin  SUN Hui  SHEN Su-jian  JIN Si-si
Affiliation:( Department of Gastroenterology, the First Affiliated Hospital of Wenzhou Medical College, Wenzhou, 325000)
Abstract:Objective: To explore the reasonability of the design of HBsAg-ecdCD40L fusionprotein. Methods: Using sequence analysis software and protocols prescribed on website www.expasy.com the open reading frame of the recombinant plasmid and the flexibility,hydrophilicity,antigenicity and epitope of recombinant HBsAg-ecdCD40L were analyzedand the secondary structure of HBsAg-ecdCD40L fusion protein was analyzed, too. Resuits: The fusion protein had correct domains of ttBsAg and ecdCD40L. The linker had low antigencity and high flexibility and might not influence the secondary structure of the fusion protein. Conclusion: The design of the fusion protein is reasonable. It Keeps the maximum biological activities of HBsAg and ecdCD40L.
Keywords:hepatitis B surface antigens  CD40 ligand  molecular structure prediction
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