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Updated: Sep 5, 2026
2-Methacryloyloxyethyl Phosphorylcholine Polymer Treatment of Complete Dentures to Inhibit Denture Plaque Deposition
Published on: December 26, 2016
A chlorinated mussel-inspired monomer stabilizes dentin via anti-proteolysis and collagen cross-linking
Na Ouyang1, Canwen Zhang2, Leqi Yang2
1School of Dentistry, Shenzhen University Medical School, Shenzhen, 518055, China; Institute of Oral Science, Shenzhen University, Shenzhen, 518055, China.
Objective:
To evaluate whether the novel monomer N-(2-chloro-4,5-dihydroxyphenethyl) methacrylamide (Cl-DMA) provides dual anti-proteolytic and collagen cross-linking effects on demineralized dentin matrices.
Methods:
A 10% ethanol/water solution served as the vehicle control, and Cl-DMA solutions were prepared at concentrations of 1, 10, and 100 mM. A 10 mM chlorhexidine acetate (CHX) solution and a 10 mM glutaraldehyde (GA) solution served as positive controls for anti-proteolytic and cross-linking effects, respectively. Inhibitory effects on matrix metalloproteinases (MMP-2, -8, -9) and Clostridium histolyticum collagenase were assessed using enzyme activity kits. In situ zymography with confocal laser scanning microscopy (CLSM) quantified MMP activity at the bonding interface. Demineralized human dentin beams treated with these solutions for 1 h were evaluated for dry mass loss, hydroxyproline release, and swelling ratio. Collagen fibril ultrastructure was observed via FESEM, while Cl-DMA/collagen binding characteristics were analyzed using ATR-FTIR spectroscopy. Molecular docking simulated the binding modes of Cl-DMA and CHX with MMPs.
Results:
Cl-DMA inhibited protease activity in a generally concentration-dependent manner. While 10 mM Cl-DMA exhibited weaker inhibition of soluble MMPs than CHX, in situ zymography revealed that 10 and 100 mM Cl-DMA significantly inhibited interfacial MMP activity, comparable to CHX. Furthermore, 100 mM Cl-DMA significantly reduced dry mass loss, hydroxyproline release, and swelling ratio. FESEM indicated decreased porosity and increased compactness of the collagen network with higher Cl-DMA concentrations. FTIR confirmed non-covalent hydrogen bond cross-linking without triple-helix disruption. Molecular docking results demonstrated that Cl-DMA could bind to MMP-2, -8, and -9, though with weaker binding affinities than CHX.
Significance:
Cl-DMA effectively inhibited protease activity and promoted collagen cross-linking and stabilization. The 100 mM concentration exhibited the greatest overall efficacy under the present experimental conditions, supporting the potential of Cl-DMA as a multifunctional dentin pretreatment agent for reducing enzymatic degradation of demineralized dentin collagen.
