Inhibitory effect of a novel crosslinking quaternary ammonium methacrylates on matrix metalloproteinases.
- Author:
Ning LIU
1
;
Fang LI
;
Ling ZHANG
;
Yu-Jiang CHEN
;
Ji-Hua CHEN
Author Information
- Publication Type:Journal Article
- MeSH: Ammonium Compounds; pharmacology; Chlorhexidine; pharmacology; Dentin; drug effects; Matrix Metalloproteinase 8; Methacrylates; chemistry
- From: Chinese Journal of Stomatology 2013;48(4):239-243
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo evaluate the anti-matrix metalloproteinase (MMP) activity of a novel crosslinking quaternary ammonium methacrylates, 2-methacryloxylethyl dodecylmethyl ammonium bromide (MAE-DB).
METHODSThe effects of MAE-DB at different concentrations (1%, 3%, 5%, 7%) on soluble matrix metalloproteinase-8 (MMP-8) were investigated using fluorescent assay kit. Readings were taken every 20 min for 3 h. The 1, 10-phenanthroline provided by the assay kit served as control group. Demineralized dentin beams were randomly divided into three groups (n = 50) and immersed in different solutions: artificial saliva, MAE-DB incorporated artificial saliva and chlorhexidine incorporated artificial saliva. After temperature cycling, the changes of ultimate tensile strength were measured to determine the effect of MAE-DB on the activity of matrix-bound endogenous matrix metalloproteinases. The morphology of dentin collagen fibrils in the three groups was observed via transmission electron microscopy (TEM).
RESULTSMAE-DB could effectively inhibit the activity of soluble MMP-8. The inhibition percentage of 3% MAE-DB was 99.53% after 1 h, and it was significantly higher than that of 1, 10-phenanthroline (95.71%, P < 0.05). After temperature cycling, the ultimate tensile strengths of MAE-DB groups were significantly higher than those of the artificial saliva groups and the chlorhexidine groups (P < 0.05). TEM micrographs of MAE-DB group revealed that the microstructure of the collagen fibrillar was intact, while the fibrillar in the artificial saliva group was disrupted, indicating a protective function of MAE-DB on dentin collagen.
CONCLUSIONSMAE-DB can inhibit the activity of MMP and protect dentin collagen from enzyme degradation.