Stress-stabilized subisostatic fiber networks in a ropelike limit.

The mechanics of disordered fibrous networks such as those that make up the extracellular matrix are strongly dependent on the local connectivity or coordination number. For biopolymer networks this coordination number is typically between 3 and 4. Such networks are sub-isostatic and linearly unstable to deformation with only central force interactions, but exhibit a mechanical phase transition between floppy and rigid states under strain.

The Role of Network Architecture in Collagen Mechanics.

Collagen forms fibrous networks that reinforce tissues and provide an extracellular matrix for cells. These networks exhibit remarkable strain-stiffening properties that tailor the mechanical functions of tissues and regulate cell behavior. Recent models explain this nonlinear behavior as an intrinsic feature of disordered networks of stiff fibers.

Elasticity of fibrous networks under uniaxial prestress.

We present theoretical and experimental studies of the elastic response of fibrous networks subjected to uniaxial strain. Uniaxial compression or extension is applied to extracellular networks of fibrin and collagen using a shear rheometer with free water in/outflow. Both uniaxial stress and the network shear modulus are measured.

Uncoupling shear and uniaxial elastic moduli of semiflexible biopolymer networks: compression-softening and stretch-stiffening.

Gels formed by semiflexible filaments such as most biopolymers exhibit non-linear behavior in their response to shear deformation, e.g., with a pronounced strain stiffening and negative normal stress.

Stress controls the mechanics of collagen networks.

Collagen is the main structural and load-bearing element of various connective tissues, where it forms the extracellular matrix that supports cells. It has long been known that collagenous tissues exhibit a highly nonlinear stress-strain relationship, although the origins of this nonlinearity remain unknown. Here, we show that the nonlinear stiffening of reconstituted type I collagen networks is controlled by the applied stress and that the network stiffness becomes surprisingly insensitive to network concentration.