RRC ID 44644
Author Ohyabu Y, Yunoki S, Hatayama H, Teranishi Y.
Title Fabrication of high-density collagen fibril matrix gels by renaturation of triple-helix collagen from gelatin.
Journal Int J Biol Macromol
Abstract Collagen-based 3-D hydrogels often lack sufficient mechanical strength for tissue engineering. We developed a method for fabrication of high-density collagen fibril matrix (CFM) gels from concentrated solutions of uncleaved gelatin (UCG). Denatured random-coil UCG exhibited more rapid and efficient renaturation into collagen triple-helix than cleaved gelatin (CG) over a broad range of setting temperatures. The UCG solution formed opaque gels with high-density reconstituted collagen fibrils at 28-32 °C and transparent gels similar to CG at <25 °C. The unique gelation properties of UCG enabled the encapsulation of cultured cells in CFM of high solid volume (>5%) and elasticity (1.28 ± 0.15 kPa at 5% and 4.82 ± 0.38 kPa at 8%) with minimal cell loss. The elastic modulus of these gels was higher than that of conventional CFM containing 0.5% collagen. High-strength CFM may provide more durable hydrogels for tissue engineering and regenerative medicine.
Volume 62
Pages 296-303
Published 2013-11-1
DOI 10.1016/j.ijbiomac.2013.09.001
PII S0141-8130(13)00474-1
PMID 24036066
MeSH Animals Cell Line Cell Survival / drug effects Collagen / chemistry* Collagen / pharmacology Gelatin / chemistry* Gels Hot Temperature Humans Protein Renaturation* Protein Structure, Secondary Temperature Tissue Engineering
IF 5.162
Times Cited 6
Human and Animal Cells UBE6T-7(RCB2157)