Collagen I is the most prevalent component of the extracellular matrix in animals, providing both structural rigidity and biological activity that is crucial in tissue organization and dynamic reorganization. Collagen I self-assembles from a solution of monomers into fibrils that may then bundle into fibers and become entangled and/or cross-linked into networks. We use confocal microscopy complementarily with rheology to probe the microstructure and mechanical properties of collagen networks both at equilibrium and as they form.  We show that two-dimensional (2D) confocal reflectance microscopy of three-dimensional (3D) collagen gels can relate network structural properties to bulk stiffness within the confines of semi-flexible polymer theory. Similar experiments performed during gelation show that percolation theory through a self-critical gel does not describe collagen network self-assembly. We use the knowledge attained in these studies to understand how topology, stiffness, and protein content independently affect cell invasion in 3D environments.

Design and characterization of collagen gels for cell migration studies

242nd National Meeting (2011)

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