目的：探讨重组毒素ＩＬ６Ｄ２４ＬｉｎｋｅｒＰＥ４０融合蛋白及其接头设计的合理性。方法：应用核酸和蛋白质序列分析软件系统ＧＯＬＤＫＥＹ软件，对ＩＬ６Ｄ２４ＬｉｎｋｅｒＰＥ４０重组毒素融合蛋白的柔性、抗原性、亲水性、表位等分子生物学特性进行计算机模拟预测，并做Ｗｅｓｔｅｒｎｂｌｏｔ分析进行验证。结果：ＩＬ６Ｄ２４ＬｉｎｋｅｒＰＥ４０分别保留了ＩＬ６Ｄ２４和ＰＥ４０的表位特征，没有新的抗原表位出现，而且柔性接头处具有极低的抗原性。Ｗｅｓｔｅｒｎｂｌｏｔ分析结果表明融合蛋白能分别与ＩＬ６和ＰＥＡ的单克隆抗体发生特异结合，这说明融合蛋白保留了ＩＬ６和ＰＥ４０的空间结构特征。结论：预测结果有助于我们更好地从实验中认识蛋白质生物活性 Objective: To investigate the rationality of the recombinant toxin IL6D24LinkerPE40 fusion protein and its linker design. Methods: Nucleic acid and protein sequence analysis software system  GOLDKEY software, IL  6D24  Linker PE40 recombinant toxin fusion protein flexibility, antigenicity, hydrophilicity, epitopes and other molecular biological characteristics of computer simulation predicted and do Westernblot analysis to verify. Results: IL6D24LinkerPE40 retained the epitope characteristics of IL6D24 and PE40, respectively. There were no new epitopes, and the antigenicity of the flexible linker was very low. Western blot analysis results show that the fusion protein and IL 6 and PEA monoclonal antibody specific binding, indicating that the fusion protein retains the IL 6 and PE40 spatial structure characteristics. Conclusion: The prediction results help us better understand the biological activity of the protein from experiments