抗体的结构决定其功能，由于目前没有西维因抗体结晶结构的解析导致其与抗原结合机理不清楚，严重影响ELISA检测技术中对抗体特异性能的改造。本研究应用分子模拟与对接技术预测西维因单链抗体的三维结构及其与西维因分子的结合模式，采用同源建模方法首先获得西维因单链抗体的三维结构，然后采用分子对接技术将三维结构模型与西维因分子进行对接。结果表明，结合过程中H-CDR2、H-CDR3和L-CDR2形成一个疏水型的凹槽，疏水型的凹槽助推西维因分子与之结合并将西维因分子牢固地卡在里面，可能的结合位点由Ala51、Ser52、Ile51、Gly54、Ser56、Arg98、Gly100等氨基酸残基组成。为深入认识西维因分子与其抗体相互作用机理提供了理论指导，并为下一步西维因单链抗体体外亲和力的成熟奠定基础。

Functions of antibody are determined by its structure. However, the interaction mechanism is still not known since no carbaryl antibody crystallization was analyzed, which severely affects its application in ELISA detection. This study aimed to predict the 3D structure and binding mode of anti-carbaryl scFv with antigen. The molecular modeling and docking technology were employed by utilizing relative bioinformatics tools and on-line resources. The results showed a hydrophobic groove was formed by H-CDR2, H-CDR3 and L-CDR2, which block in carbaryl firmly. The binding site was composed of Ala51, Ser52, Ile51, Gly54, Ser56, Arg98 and Gly100, etc. These data highlighted the mechanism of interaction between anti-carbaryl antibody and antigen. Furthermore, it provides guidance for in vitro affinity maturation of anti-carbaryl antibody.

国家自然科学基金资助项目（20905058）