Assessment of cell viability in a three-dimensional enzymatically cross-linked collagen scaffold

Yolanda Garcia, Russell Collighan, Martin Griffin, Abhay S. Pandit

Research output: Contribution to journalArticlepeer-review


Microbial transglutaminase (mTGase) is an enzyme that introduces a covalent bond between peptide bound glutamine and lysine residues. Proteins cross-linked in this manner are often more resistant to proteolytic degradation and show increased tensile strength. This study evaluates the effects of mTGase mediated cross-linking of collagen on the cellular morphology, behaviour and viability of murine 3T3 fibroblasts following their seeding into collagen scaffolds. Additionally, cell mediated scaffold contraction, porosity and level of cross-linking of the scaffold has been analysed using image analysis software, scanning electron microscopy (SEM), colorimetric assays, and Fourier transform infrared spectroscopy (FTIR). We demonstrate that the biocompatibility and cellular morphology, when comparing cultures of fibroblasts integrated in mTGase cross-linked collagen scaffolds with the native collagen counterparts, remained unaffected. It has been also elicited that the structural characteristics of collagen have been preserved while introducing enzymatically resistant covalent bonds.
Original languageEnglish
Pages (from-to)1991-2001
Number of pages11
JournalJournal of Materials Science : Materials in Medicine
Issue number10
Publication statusPublished - Oct 2007


  • Microbial transglutaminase
  • mTGase
  • enzyme
  • peptide bound glutamine
  • lysine residues
  • proteolytic degradation
  • tensile strength
  • collagen
  • cellular morphology
  • murine 3T3 fibroblasts
  • scaffolds


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