Preventing enzymatic degradation of demineralized dentin collagen using a natural crosslinker

To evaluate effectiveness of cinnamaldehyde, vanillin and dialdehyde starch in stabilizing collagen in demineralized dentin against enzymatic degradation.

Demineralized dentin collagen films were prepared from human teeth and treated for 3 min with 4% cinnamaldehyde, 4% vanillin or 4% dialdehyde starch. Deionized water and 4% glutaraldehyde served as negative and positive control. Crosslinker-collagen interaction was analysed using Fourier transform infrared spectroscopy (FTIR) (3 samples per group). After enzymatic degradation with collagenase type II, degradation was assessed via hydroxyproline assay (16 samples per group). Collagen network ultrastructure was examined using transmission electron microscopy (TEM) (2 samples per group). Data were analysed using the Kruskal-Wallis test and Dunn's multiple comparison (p = 0.05).

FTIR confirmed that cinnamaldehyde, vanillin and dialdehyde starch did not disrupt the collagen triple-helix. Hydroxyproline release (µg) from dentin treated with water, vanillin, cinnamaldehyde, dialdehyde starch and glutaraldehyde were 15.5 ± 6.4, 13.6 ± 8.0, 11.1 ± 6.7, 6.1 ± 4.3 and 0.9 ± 0.8 (water, vanillin, cinnamaldehyde > dialdehyde starch, glutaraldehyde; p < 0.05). TEM revealed intact collagen fibrils in dentin treated with glutaraldehyde and dialdehyde starch, but not the dentin treated with water, vanillin and cinnamaldehyde.

Among the three naturally derived aldehydes, this laboratory study showed that dialdehyde starch could be a promising cross-linking agent to stabilize demineralized dentin collagen.

Incorporating natural crosslinkers such as dialdehyde starch into preventive strategies may improve the preservation of demineralized dentin by stabilizing the collagen matrix.