Hepatitis B surface antigen-CD40L extracellular domain fusion protein design and prediction of biological activity.docVIP

 PAGE \* MERGEFORMAT 12 Hepatitis B surface antigen-CD40L extracellular domain fusion protein design and prediction of biological activity Of: Lin Xian Fan, Wu Jinming, Chen Jin, Sun Hui, Shen Su Jian, Jin Sisi [Abstract] Objective: To investigate the hepatitis B surface antigen-CD40L fusion protein of the extracellular domain of the design is reasonable. Methods: Gene Construction kit 2.5, DNAStar software, and Web site analysis program analysis of recombinant open reading frame and fusion protein flexibility, hydrophilicity, antigenicity, epitope and other properties, and made a secondary structure model. Results: Recombinant CMV promoter downstream of a complete gene ORF, the fusion protein secondary structure level no new antigenicity and epitope, hydrophilic unchanged, Linker parts of antigen is low, neutral and flexible high, does not affect the both ends of the fusion protein of protein secondary structure and conformation. Conclusion: rational design of recombinant fusion protein is very likely hepatitis B surface antigen and retained the CD40L extracellular domain of the biological activity, as a theoretical basis for further study. [Keywords:] Hepatitis B virus surface antigen CD40 ligand structure prediction Abstract: Objective: To explore the reasonability of the design of HBsAg-ecdCD40L fusion protein. Methods: Using sequence analysis software and protocols prescribed on website the open reading frame of the recombinant plasmid and the flexibility, hydrophilicity, antigenicity and epitope of recombinant HBsAg-ecdCD40L were analyzed and the secondary structure of HBsAg-ecdCD40L fusion protein was analyzed, too. Results: The fusion protein had correct domains of HBsAg 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. Keyword