2010/09/02 by Peng Chen, Chen, Peng, Vivek B. Shenoy +1
Biochemistry, Genetics and Molecular Biology · Medicine · Physics and Astronomy · #Biological Physics (physics.bio-ph) #Cardiomyopathy and Myosin Studies #Cellular Mechanics and Interactions #FOS: Physical sciences #Force Microscopy Techniques and Applications #Soft Condensed Matter (cond-mat.soft)
paper · pdf · doi:10.48550/arxiv.1009.0548
openalex publication_date 2010/09/02 · openalex created_date 2019/06/27 · openalex updated_date 2026/07/28
We have studied the elastic response of actin networks with both compliant and rigid crosslinks by modeling molecular motors as force dipoles. Our finite element simulations show that for compliant crosslinkers such as filamin A, the network can be stiffened by two orders of magnitude while stiffening achieved with incompliant linkers such as scruin is significantly smaller, typically a factor of two, in excellent agreement with recent experiments. We show that the differences arise from the fact that the motors are able to stretch the compliant crosslinks to the fullest possible extent, which in turn causes to the deformation of the filaments. With increasing applied strain, the filaments further deform leading to a stiffened elastic response. When the crosslinks are incompliant, the contractile forces due to motors do not alter the network morphology in a significant manner and hence only small stiffening is observed.