Multiscale Insights of Domain Unfolding in Fibrin Mechanical Response (2503.24315v1)

Abstract: Fibrinogen, the monomeric unit of fibrin, the main constituent of blood clot, has a very complex structure. The fibrinogen builds the fibrin fiber and network through the half-staggered packing via knob-hole interaction and the $\alpha$C crosslinkers. Due to its rich structure, the elastic behavior also shows a unique nature of very high stretchability and multiple regimes in stress-strain behaviour, which is not yet fully understood. We develop an Unfolding-incorporated Coarse-Grained Polymer (UCGP) model for fibrinogen to study the effect of domain unfolding on the mechanical behavior of fibrin fiber and network. Our model captures the stretching behavior of fibrinogen as observed in AFM and all-atom simulations. We further extend our model to fibrin fiber to study the effect of molecular unfolding at the fiber and network level. We anticipate that our model will be able to account for the nonlinear mechanical behavior of crosslinked fibrin gel. It is possibly the first model of this sort to consider the precise, controllable knowledge of the effects of domain unfolding in crosslinked proteins. This model can also be used to model systems that have sacrificial bonds.