TY - JOUR
T1 - Physical, Biomechanical, and Optical Characterization of Collagen and Elastin Blend Hydrogels
AU - Vazquez-Portalatin, Nelda
AU - Alfonso-Garcia, Alba
AU - Liu, Julie C.
AU - Marcu, Laura
AU - Panitch, Alyssa
PY - 2020
Y1 - 2020
N2 - 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.
AB - 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.
KW - Autofluorescence lifetime
KW - D-banding pattern
KW - Fibrillogenesis
KW - FLIm
KW - Storage modulus
UR - http://www.scopus.com/inward/record.url?scp=85090936854&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85090936854&partnerID=8YFLogxK
U2 - 10.1007/s10439-020-02605-x
DO - 10.1007/s10439-020-02605-x
M3 - Article
C2 - 32929559
AN - SCOPUS:85090936854
JO - Annals of Biomedical Engineering
JF - Annals of Biomedical Engineering
SN - 0090-6964
ER -