【摘要】 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。更多还原

【Abstract】 To reveal the molecular interaction model between fumonisin B1(FB1) and its specific single chain variable fragment(scFv) antibody, the three dimensional structure of an anti-FB1 scFv antibody was modeled and refined using homology modeling for molecular docking analysis. Procheck and Verify 3D methods were used to confirm the reliability of the scFv conformation. The recognition and interaction including hydrogen bonding,hydrophobic and electrostatic properties between the scFv antibody and FB1 were analyzed by molecular docking method. The results showed that the complementarity-determining regions(CDRs) of the scFv antibody directly face FB1 molecule in the antibody-antigen complex. The hydrogen bonds are steadily formed between the scFv and its antigen; also the hydrophobic interaction and electrostatic matching of the scFv antibody are in good complementary with FB1 molecule. In conclusion, the effects of hydrogen bonding, electrostatic and hydrophobic interaction together make the scFv antibody forming a favorable binding pocket that is highly complementary to FB1, and this unique feature plays a vital role in the specific recognition and binding stability of antibody-antigen complex.更多还原