The antigen-antibody unbinding process through steered molecular dynamics of a complex of an Fv fragment and lysozyme
The antigen-antibody unbinding process through steered molecular dynamics of a complex of an Fv fragment and lysozyme
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DOI：
10.1088/0953-8984/20/25/255238
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发表时间：
2008-06-25
影响因子：
2.7
通讯作者：
Kawano, Satoyuki
中科院分区：
文献类型：
--
作者：
Hanasaki, Itsuo;Haga, Tomoaki;Kawano, Satoyuki
我们已经研究了抗原-抗体的解结合过程中使用转向分子动力学（SMD）模拟。我们专注于由抗体分子的Fv片段和作为抗原分子的溶菌酶组成的复杂系统。Fv片段由VL和VH链组成。结果表明，VH链比VL链更早地被解结合，这通过从40个解结合轨迹获得的距离分布的系综平均值证实。使用溶菌酶作为抗原分子而不是小的半抗原分子揭示了这样的事实，即通过伴随解结合过程的变形来估计的诱导拟合对于抗原分子比对于抗体分子更显著。SMD还揭示了解绑过程所需的最大力的非高斯分布。
We have investigated the antigen-antibody unbinding process using steered molecular dynamics (SMD) simulations. We focus on a complex system consisting of an Fv fragment of an antibody molecule and a lysozyme as an antigen molecule. The Fv fragment consists of a VL and VH chain. The results show that the VH chain is unbound earlier than the VL chain, which is confirmed by the ensemble average of the distance profile obtained from 40 unbinding trajectories. The use of lysozyme as an antigen molecule instead of a small hapten molecule reveals the fact that the induced fit, estimated by the deformation accompanying the unbinding process, is more noticeable for the antigen molecule than for the antibody molecule. The SMD also reveals the non-Gaussian distribution of maximum force necessary for the unbinding process.