Physical, Biomechanical, and Optical Characterization of Collagen and Elastin Blend Hydrogels

Collagen and elastin proteins are major components of the extracellular matrix of many organs. The presence of collagen and elastin networks, and their associated properties, in different tissues have led scientists to study collagen and elastin composites for use in tissue engineering. In this study, we characterized physical, biochemical, and optical properties of gels composed of collagen and elastin blends. We demonstrated that the addition of varying amounts of elastin to the constructs alters collagen fibrillogenesis, D-banding pattern length, and storage modulus. However, the addition of elastin does not affect collagen fibril diameter. We also evaluated the autofluorescence properties of the different collagen and elastin blends with fluorescence lifetime imaging (FLIm). Autofluorescence emission showed a red shift with the addition of elastin to the hydrogels. The fluorescence lifetime values of the gels increased with the addition of elastin and were strongly correlated with the storage moduli measurements. These results suggest that FLIm can be used to monitor the gels' mechanical properties nondestructively. These collagen and elastin constructs, along with the FLIm capabilities, can be used to develop and study collagen and elastin composites for tissue engineering and regenerative medicine.