The anti-MMP activity of benzalkonium chloride

Arzu Tezvergil-Mutluay, M. Murat Mutluay, Li Sha Gu, Kai Zhang, Kelli A. Agee, Ricardo M. Carvalho, Adriana Manso, Marcela Carrilho, Franklin R. Tay, Lorenzo Breschi, Byoung In Suh, David H. Pashley

Research output: Contribution to journalArticle

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Abstract

Objective: This study evaluated the ability of benzalkonium chloride (BAC) to bind to dentine and to inhibit soluble recombinant MMPs and bound dentine matrix metalloproteinases (MMPs). Methods: Dentine powder was prepared from extracted human molars. Half was left mineralized; the other half was completely demineralized. The binding of BAC to dentine powder was followed by measuring changes in the supernatant concentration using UV spectrometry. The inhibitory effects of BAC on rhMMP-2,-8 and-9 were followed using a commercially available in vitro proteolytic assay. Matrix-bound endogenous MMP-activity was evaluated in completely demineralized beams. Each beam was either dipped into BAC and then dropped into 1 mL of a complete medium (CM) or they were placed in 1 mL of CM containing BAC for 30 days. After 30 days, changes in the dry mass of the beams or in the hydroxyproline (HYP) content of hydrolysates of the media were quantitated as indirect measures of matrix collagen hydrolysis by MMPs. Results: Demineralized dentine powder took up 10-times more BAC than did mineralized powder. Water rinsing removed about 50% of the bound BAC, whilst rinsing with 0.5 M NaCl removed more than 90% of the bound BAC. BAC concentrations 0.5 wt% produced 100% inhibition of soluble recombinant MMP-2,-8 or-9, and inhibited matrix-bound MMPs between 55 and 66% when measured as mass loss or 76-81% when measured as solubilization of collagen peptide fragments. Conclusions: BAC is effective at inhibiting both soluble recombinant MMPs and matrix-bound dentine MMPs in the absence of resins.

Original languageEnglish (US)
Pages (from-to)57-64
Number of pages8
JournalJournal of Dentistry
Volume39
Issue number1
DOIs
StatePublished - Jan 1 2011

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Benzalkonium Compounds
Matrix Metalloproteinases
Dentin
Powders
Collagen
Matrix Metalloproteinase 8
Peptide Fragments
Matrix Metalloproteinase 2
Hydroxyproline
Spectrum Analysis
Hydrolysis

Keywords

  • Benzalkonium chloride
  • Binding
  • Dentine
  • MMPs

ASJC Scopus subject areas

  • Dentistry(all)

Cite this

Tezvergil-Mutluay, A., Mutluay, M. M., Gu, L. S., Zhang, K., Agee, K. A., Carvalho, R. M., ... Pashley, D. H. (2011). The anti-MMP activity of benzalkonium chloride. Journal of Dentistry, 39(1), 57-64. https://doi.org/10.1016/j.jdent.2010.10.003

The anti-MMP activity of benzalkonium chloride. / Tezvergil-Mutluay, Arzu; Mutluay, M. Murat; Gu, Li Sha; Zhang, Kai; Agee, Kelli A.; Carvalho, Ricardo M.; Manso, Adriana; Carrilho, Marcela; Tay, Franklin R.; Breschi, Lorenzo; Suh, Byoung In; Pashley, David H.

In: Journal of Dentistry, Vol. 39, No. 1, 01.01.2011, p. 57-64.

Research output: Contribution to journalArticle

Tezvergil-Mutluay, A, Mutluay, MM, Gu, LS, Zhang, K, Agee, KA, Carvalho, RM, Manso, A, Carrilho, M, Tay, FR, Breschi, L, Suh, BI & Pashley, DH 2011, 'The anti-MMP activity of benzalkonium chloride', Journal of Dentistry, vol. 39, no. 1, pp. 57-64. https://doi.org/10.1016/j.jdent.2010.10.003
Tezvergil-Mutluay A, Mutluay MM, Gu LS, Zhang K, Agee KA, Carvalho RM et al. The anti-MMP activity of benzalkonium chloride. Journal of Dentistry. 2011 Jan 1;39(1):57-64. https://doi.org/10.1016/j.jdent.2010.10.003
Tezvergil-Mutluay, Arzu ; Mutluay, M. Murat ; Gu, Li Sha ; Zhang, Kai ; Agee, Kelli A. ; Carvalho, Ricardo M. ; Manso, Adriana ; Carrilho, Marcela ; Tay, Franklin R. ; Breschi, Lorenzo ; Suh, Byoung In ; Pashley, David H. / The anti-MMP activity of benzalkonium chloride. In: Journal of Dentistry. 2011 ; Vol. 39, No. 1. pp. 57-64.
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abstract = "Objective: This study evaluated the ability of benzalkonium chloride (BAC) to bind to dentine and to inhibit soluble recombinant MMPs and bound dentine matrix metalloproteinases (MMPs). Methods: Dentine powder was prepared from extracted human molars. Half was left mineralized; the other half was completely demineralized. The binding of BAC to dentine powder was followed by measuring changes in the supernatant concentration using UV spectrometry. The inhibitory effects of BAC on rhMMP-2,-8 and-9 were followed using a commercially available in vitro proteolytic assay. Matrix-bound endogenous MMP-activity was evaluated in completely demineralized beams. Each beam was either dipped into BAC and then dropped into 1 mL of a complete medium (CM) or they were placed in 1 mL of CM containing BAC for 30 days. After 30 days, changes in the dry mass of the beams or in the hydroxyproline (HYP) content of hydrolysates of the media were quantitated as indirect measures of matrix collagen hydrolysis by MMPs. Results: Demineralized dentine powder took up 10-times more BAC than did mineralized powder. Water rinsing removed about 50{\%} of the bound BAC, whilst rinsing with 0.5 M NaCl removed more than 90{\%} of the bound BAC. BAC concentrations 0.5 wt{\%} produced 100{\%} inhibition of soluble recombinant MMP-2,-8 or-9, and inhibited matrix-bound MMPs between 55 and 66{\%} when measured as mass loss or 76-81{\%} when measured as solubilization of collagen peptide fragments. Conclusions: BAC is effective at inhibiting both soluble recombinant MMPs and matrix-bound dentine MMPs in the absence of resins.",
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