The inhibitory effects of quaternary ammonium methacrylates on soluble and matrix-bound MMPs

Department of Prosthodontics and Turku Clinical Biomaterials Center, University of Turku, Institute of Dentistry, Lemminkaisenkatu 2, FI-20520 Turku, Finland.
Journal of dental research (Impact Factor: 4.14). 03/2011; 90(4):535-40. DOI: 10.1177/0022034510389472
Source: PubMed

ABSTRACT 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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Available from: Arzu Tezvergil, Aug 14, 2015
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    • "Attempts have been focused on inhibition of the protease activity to increase the durability of resin dentin bonds [10]. Recently, quaternary ammonium compounds (QACs), well recognized antibacterial agents, have been reported to be effective on inhibiting endogenous dentin proteases [11] [12]. Benzalkonium chloride (BAC), which is a QAC, was previously shown to bind strongly to demineralized dentin and inhibit soluble and matrix-bound MMPs [12]. "
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    • "A low pH alters the conformation of the protein, and induces the cysteine switch that activates the catalytic activity [112] [113] [114]. Therefore, MMPs may become activated during acid etching , or upon bacterial acid production at the tooth and restoration interface [105] [112]. With large quantities of water present in the dentin and saliva, activated MMPs are able to hydrolyze the collagen, and compromise the stability of the resin–dentin interface [111]. "
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