Investigating the effect of different transducer stiffness values on the contactin complex detachment by steered molecular dynamics

摘要

Graphical abstract Display Omitted Highlights ? CNTN4-PTPRG complex is studied by SMD. ? Effects of different accessible parameters on rupture forces were investigated. ? The results showed the dependence of rupture force on transducer stiffness and pulling velocities. ? The lowest transducer stiffness showed interesting behavior about bond lifetime and non-constant pulling velocity mode. Abstract This study investigated the adhesion behavior of Contactin4 (CNTN4), a member of Immunoglobulin Super Family (Ig-SF) of cell adhesion molecules. Contactin4 plays a crucial role in the formation, maintenance, and plasticity of neuronal networks. Contactin in its complex configuration with protein tyrosine phosphatase gamma (PTPRG) was selected for simulation. By utilizing Steered Molecular Dynamics (SMD), the uniaxial force was applied to induce unbinding of the complex, and the force-induced detachment of complex components was probed. Three sets of simulations with three values of transducer stiffness and five pulling speeds were designed. Our results showed the dependence of unbinding force on both accessible parameters of pulling speed and spring stiffness. By increasing the stiffness value and pulling speed the rupture force increased. Accordingly, the dissociation rates due to the Bell’s theory based on rupture forces and loading rates were calculated. ]]>