Influence of collagen source on fibrillar architecture and properties of vitrified collagen membranes

J Biomed Mater Res B Appl Biomater. 2016 Feb;104(2):300-7. doi: 10.1002/jbm.b.33381. Epub 2015 Mar 12.


Collagen vitrigel membranes are transparent biomaterials characterized by a densely organized, fibrillar nanostructure that show promise in the treatment of corneal injury and disease. In this study, the influence of different type I collagen sources and processing techniques, including acid-solubilized collagen from bovine dermis (Bov), pepsin-solubilized collagen from human fibroblast cell culture (HuCC), and ficin-solubilized collagen from recombinant human collagen expressed in tobacco leaves (rH), on the properties of the vitrigel membranes was evaluated. Postvitrification carbodiimide crosslinking (CX) was also carried out on the vitrigels from each collagen source, forming crosslinked counterparts BovXL, HuCCXL, and rHXL, respectively. Collagen membrane ultrastructure and biomaterial properties were found to rely heavily on both collagen source and crosslinking. Bov and HuCC samples showed a random fibrillar organization of collagen, whereas rH vitrigels showed remarkable regional fibril alignment. After CX, light transmission was enhanced in all groups. Denaturation temperatures after CX increased in all membranes, of which the highest increase was seen in rH (14.71°C), suggesting improved thermal stability of the collagen fibrils in the membranes. Noncrosslinked rH vitrigels may be reinforced through CX to reach levels of mechanical strength and thermal stability comparable to Bov.

Keywords: cornea/conjunctiva; extracellular matrix; eye; ocular.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Cattle
  • Collagen / chemistry*
  • Dermis / chemistry
  • Humans
  • Membranes, Artificial*
  • Recombinant Proteins / chemistry
  • Vitrification*


  • Membranes, Artificial
  • Recombinant Proteins
  • Collagen