Journal
JOURNAL OF DENTAL RESEARCH
Volume 90, Issue 4, Pages 535-540Publisher
SAGE PUBLICATIONS INC
DOI: 10.1177/0022034510389472
Keywords
dentin; hydroxyproline; MDPB; matrix metalloproteinase; quaternary ammonium methacrylates
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Funding
- Kuraray Medical Inc.
- National Institute of Dental and Craniofacial Research (NIDCR) [R01 DE015306-06]
- Academy of Finland [8126472]
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Matrix metalloproteinases (MMPs) bound to dentin contribute to the progressive degradation of collagen fibrils in hybrid layers created by dentin adhesives. This study evaluated the MMP-inhibiting potential of quaternary ammonium methacrylates (QAMs), with soluble rhMMP-9 and a matrix-bound endogenous MMP model. Six different QAMs were initially screened by a rhMMP-9 colorimetric assay. For the matrix-bound endogenous MMPs, we aged demineralized dentin beams for 30 days in calcium-and zinc-containing media (CM; control), chlorhexidine, or QAMs in CM to determine the changes in dry mass loss and solubilization of collagen peptides against baseline levels. The inhibitory effects of QAMs on soluble rhMMP-9 varied between 34 and 100%. Beams incubated in CM showed a 29% decrease in dry mass (p < 0.05), whereas beams incubated with QAMs showed only 0.2%-6% loss of dry mass. Significantly more solubilized collagen was detected from beams incubated in CM (p < 0.05). It is concluded that QAMs exhibited dentin MMP inhibition comparable with that of chlorhexidine, but required higher concentrations.
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