  The synthetic actin network demands great interest as bio-material due to its
soft and wet nature that mimic many biological scaffolding structures. The
study of these structures can contribute to a better understanding of this new
micro/nano technology and the cytoskeleton like structural building blocks.
Inside the cell the actin network is regulated by tens of actin-binding
proteins (ABP's), which makes for a highly complex system with several emergent
behavior. In particular Calponin is an ABP that was identified as an actin
stabiliser, but its mechanism is poorly understood. Recent experiments using an
in vitro model system of cross-linked actin with Calponin and large deformation
bulk rheology, found that networks with basic calponin exhibited a delayed
onset and were able to withstand a higher maximal strain before softening.
  In this work we propose a mathematical model into the framework of nonlinear
continuum mechanics to explain the observation of Jansen, where we introduce
the hypothesis by which the difference between the two networks, with and
without Calponin, is interpreted as a alterations in the pre-strain developed
by the network entanglement and the regulation of the crosslinks adhesion
energy. The mechanics of the F-actin is modelled using the wormlike chain model
for semi-flexible filaments and the gelation process is described as mesoscale
dynamics for the crosslinks. The model has been validated with reported
experimental results from literature, showing a good agreement between theory
and experiments.
