Elastic regimes of subisostatic athermal fiber networks

Phys Rev E. 2016 Jan;93(1):012407. doi: 10.1103/PhysRevE.93.012407. Epub 2016 Jan 14.

Abstract

Athermal models of disordered fibrous networks are highly useful for studying the mechanics of elastic networks composed of stiff biopolymers. The underlying network architecture is a key aspect that can affect the elastic properties of these systems, which include rich linear and nonlinear elasticity. Existing computational approaches have focused on both lattice-based and off-lattice networks obtained from the random placement of rods. It is not obvious, a priori, whether the two architectures have fundamentally similar or different mechanics. If they are different, it is not clear which of these represents a better model for biological networks. Here, we show that both approaches are essentially equivalent for the same network connectivity, provided the networks are subisostatic with respect to central force interactions. Moreover, for a given subisostatic connectivity, we even find that lattice-based networks in both two and three dimensions exhibit nearly identical nonlinear elastic response. We provide a description of the linear mechanics for both architectures in terms of a scaling function. We also show that the nonlinear regime is dominated by fiber bending and that stiffening originates from the stabilization of subisostatic networks by stress. We propose a generalized relation for this regime in terms of the self-generated normal stresses that develop under deformation. Different network architectures have different susceptibilities to the normal stress but essentially exhibit the same nonlinear mechanics. Such a stiffening mechanism has been shown to successfully capture the nonlinear mechanics of collagen networks.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biopolymers / chemistry*
  • Collagen / chemistry
  • Elasticity*
  • Humans
  • Linear Models
  • Models, Molecular*
  • Nonlinear Dynamics
  • Stress, Mechanical

Substances

  • Biopolymers
  • Collagen