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

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Annals of Biomedical Engineering ( 2020) https://doi.org/10.1007/s10439-020-02605-x

Original Article

Physical, Biomechanical, and Optical Characterization of Collagen and Elastin Blend Hydrogels NELDA VAZQUEZ-PORTALATIN,1,2 ALBA ALFONSO-GARCIA,1 JULIE C. LIU,2,3 LAURA MARCU,1 and ALYSSA PANITCH 1,4 1

Biomedical Engineering Department, University of California, Davis, 451 Health Sciences Dr, Davis, CA 95616, USA; 2Weldon School of Biomedical Engineering, Purdue University, 206 S Martin Jischke Dr, West Lafayette, IN 47907, USA; 3Davidson School of Chemical Engineering, Purdue University, 480 Stadium Mall Dr, West Lafayette, IN 47907, USA; and 4Department of Surgery, University of California, Davis, 2335 Stockton Boulevard, Sacramento, CA 95817, USA (Received 27 May 2020; accepted 2 September 2020) Associate Editor Michael S. Detamore oversaw the review of this article.

Abstract—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. Keywords—Fibrillogenesis, D-banding pattern, modulus, FLIm, Autofluorescence lifetime.

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Address correspondence to Alyssa Panitch, Department of Surgery, University of California, Davis, 2335 Stockton Boulevard, Sacramento, CA 95817, USA. Electronic mail: [email protected]

INTRODUCTION Collagen has been extensively used in tissue engineering due to its biocompatibility, abundant presence in body tissues, and wide clinical approval.5,21,25,26,28 However, collagen constructs do not fully mimic the complex composition, network, and biochemical and biomechanical properties observed in native tissues.5 Previous work has focused on the addition of other extracellular matrix (ECM) components, particularly elastin,6,14,15,18,31,45,48,55 chondroitin sulfate,14,17,20,57,60,61,63 and hyaluronic acid,32,47,48,57,63 to collagen-based constructs