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目的分析伏马菌素B1(Fumonisin B1,FB1)与其特异单链抗体的分子互作模式。方法通过同源建模构建和优化抗FB1单链抗体的三维结构,结合Procheck和Verify 3D等方法评价得到稳定的抗体模型,利用分子对接研究单链抗体与其抗原FB1的结合特性、疏水性和表面静电力作用。结果单链抗体的互补决定区参与同其抗原FB1的结合,抗体与抗原之间不仅形成稳定的氢键,疏水性和静电力的匹配也很好。结论氢键结合力、分子间疏水相互作用和静电力的共同作用,使得单链抗体形成一个能够与FB1高度互补的相互作用区域,并在抗体与抗原的特异性识别及结合稳定性等方面起着关键作用。
Objective To analyze the molecular interaction pattern of Fumonisin B1 (FB1) and its specific single chain antibody. Methods The three-dimensional structure of anti-FB1 scFv was constructed and optimized by homology modeling. The stable antibody model was evaluated by the methods of Procheck and Verify 3D. The molecular docking was used to study the binding properties of single chain antibody to its antigen FB1, hydrophobicity and surface Electrostatic force effect. Results Complementarity determining region of single chain antibody was involved in the binding with its antigen FB1, not only stable hydrogen bond was formed between antibody and antigen, but also hydrophobicity and electrostatic force were well matched. Conclusions Hydrogen bonding, intermolecular hydrophobic interaction and electrostatic interaction make the scFv form a highly complementary region of interaction with FB1 and play an important role in the specific recognition of antibody and antigen and the stability of binding The key role.