表皮生长因子受体（EGFR）是HER受体家族的一员，在各种癌细胞中过度表达。使用肿瘤特异性抗体将细胞毒素直接输送到肿瘤细胞中是一种有效的治疗策略。将抗EGFR scFv与肿瘤特异性细胞因子融合的靶向治疗有望开启新时代。我们设计了一种新型免疫凋亡融合蛋白，抗EGFR scFv-IL-24，由特异性癌细胞靶向抗体和重组细胞因子IL-24组成，探索其抗癌潜力。利用特定刚性连接器将抗EGFR scFv和IL-24的氨基酸序列融合在一起。使用在线生物信息学工具进行了设计的融合蛋白的原位性、次级性、生物物理性质、质量和结构验证的基础特征化。新设计的融合蛋白由402个氨基酸组成，在ERRAT2和Ramachandran图分析预测下，质量预测值为76.7%，最优位置的残基占81.5%。使用HDOCK和Schrodinger的Desmond模块进行了对接和模拟研究。质量、有效性、相互作用分析和稳定性的所有参数均表明融合分子是完全可操作和功能性的。研究结果支持抗EGFR scFv-IL-24融合蛋白可能成为一个新的抗癌候选物。© 2023. 作者，独家授权给 Springer-Verlag GmbH Germany，Springer Nature 的一部分。

Epidermal growth factor receptor (EGFR), a member of the HER receptor family, is over expressed in various cancer cells. Using tumor-specific antibodies to deliver cytotoxic agents directly to the tumor cells is an effective treatment strategy. Targeted therapy by fusing anti-EGFR scFv with tumor-specific cytokines promises the emergence of a new era.We designed a novel immuno-apoptotic fusion protein, anti-EGFR scFv-IL-24, consisting of a specific cancer cell targeting antibody and recombinant cytokine IL-24 to explore its anti-cancerous potential. Amino acid sequences of both anti-EGFR scFv and IL-24 were fused using a specific rigid linker. In silico characterization of the designed fusion protein like to predict the primary, secondary, physiochemical properties, quality, and structural validation using online bioinformatic tools. The newly designed fusion protein consists of 402 amino acids that showed good quality with a predicted value of 76.7% having 81.5% residues in the most favored region as predicted by ERRAT2 and Ramachandran plot analysis. Docking and simulation studies were performed using HDOCK and Desmond module of Schrodinger. All the parameters of quality, validity, interaction analysis, and stability suggested that the fused molecule is fully operational and functional. The results of the study support that the anti-EGFR scFv-IL-24 fused protein could be proved as a novel candidate to combat cancer.© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.