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Tissue Engineering (United States) 2006-06-01

Characterization of a microbial transglutaminase cross-linked type II collagen scaffold.

Damien M O Halloran, Russell J Collighan, Martin Griffin, Abhay S Pandit

文献索引:Tissue Eng. 12(6) , 1467-74, (2006)

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摘要

This study investigated the effect on the mechanical and physicochemical properties of type II collagen scaffolds after cross-linking with microbial transglutaminase (mTGase). It is intended to develop a collagen-based scaffold to be used for the treatment of degenerated intervertebral discs. By measuring the amount of epsilon-(gamma-glutamyl)lysine isodipeptide formed after cross-linking, it was determined that the optimal enzyme concentration was 0.005% (w/v). From the production of covalent bonds induced by mTGase cross-linking, the degradation resistance of type II collagen scaffolds can be enhanced. Rheological analysis revealed an almost sixfold increase in storage modulus (G') with 0.005% (w/v) mTGase cross-linked scaffolds (1.31 +/- 0.03 kPa) compared to controls (0.21 +/- 0.01 kPa). There was a significant reduction in the level of cell-mediated contraction of scaffolds with increased mTGase concentrations. Cell proliferation assays showed that mTGase crosslinked scaffolds exhibited similar cytocompatibility properties in comparison to non-cross-linked scaffolds. In summary, cross-linking type II collagen with mTGase imparted more desirable properties, making it more applicable for use as a scaffold in tissue engineering applications.

相关化合物

结构式 名称/CAS号 全部文献
Epsilon-(gamma-glutamyl)-lysine 结构式 Epsilon-(gamma-glutamyl)-lysine
CAS:17105-15-6