Effects of domain unfolding and catch-like dissociation on the collective behavior of integrin-fibro

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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 inter-facial 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.,catch-like 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.
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