Extracellular matrix (ECM) proteins (e.g. collagen, elastin) play an important role in biological tissues. In addition to conferring mechanical strength to a tissue, the ECM provides a biochemical environment essential for modulation of cellular responses such as growth and migration. Collagens are the dominant protein of the ECM, with collagen type I being most abundant. Our group and others have shown that the mechanical properties of a collagen I matrix change with collagen concentration, and when formed in the presence of a secondary fibril network such as fibrin [1]. We are interested in collagen-fibrin systems because our group uses fibrin as the starting scaffold material for cardiovascular tissue engineering, which produces interpenetrating collagen-fibrin matrices during the remodeling process as the fibrin network is degraded and replaced with cell-deposited collagen [2]. Fibrin and collagen networks are also present together around the thrombus during the wound healing process. Research has shown that ECM mechanical properties are correlated with their overall network structure characteristics such as fibril diameter [3]. Currently we have a modeling framework that generates an ECM microstructural network which can be used to predict the overall properties of a bioengineered tissue [4]. This framework allows exploration of the structure-function relation, but how the structure depends on composition remains poorly understood, especially in multi-component gels. Thus, the objective of this work was to quantify the collagen network architecture in pure collagen gels of different concentrations and in collagen-fibrin co-gels.

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