Characterization of Genipin-Modified Dentin Collagen

Abstract EN

Application of biomodification techniques to dentin can improve its biochemical and biomechanical properties.

Several collagen cross-linking agents have been reported to strengthen the mechanical properties of dentin.

However, the characteristics of collagen that has undergone agent-induced biomodification are not well understood.

The objective of this study was to analyze the effects of a natural cross-linking agent, genipin (GE), on dentin discoloration, collagen stability, and changes in amino acid composition and lysyl oxidase mediated natural collagen cross-links.

Dentin collagen obtained from extracted bovine teeth was treated with three different concentrations of GE (0.01%, 0.1%, and 0.5%) for several treatment times (0–24 h).

Changes in biochemical properties of NaB3H4-reduced collagen were characterized by amino acid and cross-link analyses.

The treatment of dentin collagen with GE resulted in a concentration- and time-dependent pigmentation and stability against bacterial collagenase.

The lysyl oxidase-mediated trivalent mature cross-link, pyridinoline, showed no difference among all groups while the major divalent immature cross-link, dehydro-dihydroxylysinonorleucine/its ketoamine in collagen treated with 0.5% GE for 24 h, significantly decreased compared to control (P< 0.05).

The newly formed GE-induced cross-links most likely involve lysine and hydroxylysine residues of collagen in a concentration-dependent manner.

Some of these cross-links appear to be reducible and stabilized with NaB3H4.