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We have studied the elastic response of actin networks with both compliantand rigid crosslinks by modeling molecular motors as force dipoles. Our finiteelement simulations show that for compliant crosslinkers such as filamin A, thenetwork can be stiffened by two orders of magnitude while stiffening achievedwith incompliant linkers such as scruin is significantly smaller, typically afactor of two, in excellent agreement with recent experiments. We show that thedifferences arise from the fact that the motors are able to stretch thecompliant crosslinks to the fullest possible extent, which in turn causes tothe deformation of the filaments. With increasing applied strain, the filamentsfurther deform leading to a stiffened elastic response. When the crosslinks areincompliant, the contractile forces due to motors do not alter the networkmorphology in a significant manner and hence only small stiffening is observed.

Strain stiffening induced by molecular motors in active crosslinked biopolymer networks