To gain more understanding of cell-matrix adhesion,we consider an idealized theoretical model of a cluster of integrin-fibronectin bonds at the cell-matrix interface subjected to a dynamic ramping.The distributions of...To gain more understanding of cell-matrix adhesion,we consider an idealized theoretical model of a cluster of integrin-fibronectin bonds at the cell-matrix interface subjected to a dynamic ramping.The distributions of bond traction and interfacial deformation are assumed to obey classical elastic equations,whereas the dissociation/association of individual bonds as well as unfolding/refolding of fibronectin domains are described by stochastic equations.Through stochastic-elasticity coupling,we perform Monte Carlo simulations to investigate how the collective behavior and adhesion performance of the integrin-fibronectin-mediated interface are influenced by two characteristics newly incorporated in the modeling,i.e.,catchlike dissociation between integrin and fibronectin,and unfolding of repeated domains in fibronectin.The probable unfolding of fibronectin domains is found to have profound effects on the resultant adhesion energy of the integrin-fibronectin-mediated interface,and governs the failure model transiting between uniform decay and catastrophic crack-like rupture.展开更多
基金This work was supported by the National Natural Science Foundation of China(Grants 11672268 and 91748209)the Fundamental Research Funds for Central Universities of China(Grant 2020XZZX005-02).
文摘To gain more understanding of cell-matrix adhesion,we consider an idealized theoretical model of a cluster of integrin-fibronectin bonds at the cell-matrix interface subjected to a dynamic ramping.The distributions of bond traction and interfacial deformation are assumed to obey classical elastic equations,whereas the dissociation/association of individual bonds as well as unfolding/refolding of fibronectin domains are described by stochastic equations.Through stochastic-elasticity coupling,we perform Monte Carlo simulations to investigate how the collective behavior and adhesion performance of the integrin-fibronectin-mediated interface are influenced by two characteristics newly incorporated in the modeling,i.e.,catchlike dissociation between integrin and fibronectin,and unfolding of repeated domains in fibronectin.The probable unfolding of fibronectin domains is found to have profound effects on the resultant adhesion energy of the integrin-fibronectin-mediated interface,and governs the failure model transiting between uniform decay and catastrophic crack-like rupture.
