The inhibitory effect of polyvinylphosphonic acid on functional matrix metalloproteinase activities in human demineralized dentin

Abstract

This study examined the use of polyvinylphosphonic acid (PVPA), as a potential matrix metalloproteinase (MMP) inhibitor and how brief cross-linking of demineralized dentin matrix that did not affected its mechanical properties enhanced the anti-MMP activity of PVPA. The anti-MMP potential of five PVPA concentrations (100-3,000 μg/mL) was initially screened using a rhMMP-9 colorimetic assay. Demineralized dentin beams were treated with the same five concentrations of PVPA to collagen and then aged for 30 days in a calcium-and zinc-containing medium. The changes in modulus of elasticity, loss of dry mass and dissolution of collagen peptides via three-point bending, precision weighing and hydroxyproline assay, respectively were measured. All tested PVPA concentrations were highly effective (p<0.05) in inhibiting MMP-9. Aging in the incubation medium did not significantly alter the modulus of elasticity of the five PVPA-treatment groups. Conversely, aged dentin beams from the control group exhibited a significant decline in their modulus of elasticity (p<0.05) over time. Mass loss from dentin beams and the corresponding increase in hydroxyproline of from the medium in the five PVPA treatment groups were significantly lower than the control (p<0.05). PVPA is a potent inhibitor of endogenous MMP activities in demineralized dentin. It may be used as an alternative to chlorhexidine for preventing collagen degradation within hybrid layers to extend the longevity of resin-dentin bonds.

Zoledronate and Ion-releasing Resins Impair Dentin Collagen Degradation

“…Indeed, analogs of non-collagenous proteins such as polyvinylphosphonic acid (PVPA) are used both to inhibit MMPs (Tezvergil-Mutluay et al, 2010) and to remineralize collagen fibrils (Tay and Pashley, 2008) and/or fossilize MMPs (Tjäderhane et al, 2013). Polyvinylphosphonic acid can diffuse and bind to specific sites along the surfaces of the collagen fibrils and along the tropocollagen molecules, thereby guiding mineral deposition within the gap regions of the collagen fibrils (Weiner, 2008).…”

“…Bioactive silicate-doped resin co-monomer blends reduce MMP-mediated matrix degradation processes due to apatite precipitation that remineralizes MMPs and the collagen matrix to which they are bound (Osorio et al, 2012). A poly(vinylphosphonic acid) such as zoledronate may provide additional MMP inhibition due to its chelation ability (Tezvergil-Mutluay et al, 2010). The combination of these 2 agents might represent a further strategy for the inhibition of endogenous proteases within the resin-dentin interface.…”

The Inhibitory Effects of Quaternary Ammonium Methacrylates on Soluble and Matrix-bound MMPs

“…However, beams incubated in simulation body fluids did lose dry mass and did solubilize collagen. Beams incubated in MMP inhibitors like chlorhexidine (Carrilho et al, 2009) or polyvinylphosphoric acid (Tezvergil-Mutluay et al, 2010) do prevent loss of dry mass and solubilization of collagen. Thus, this simple in vitro model is very useful in such studies.…”

“…The collagen in demineralized dentin is insoluble type I collagen (Carrilho et al, 2009;Tezvergil-Mutluay et al, 2010). Demineralization of the mineralized dentin matrix with 10% phosphoric acid exposes and activates endogenous MMPs, even though they remain bound to the collagen (Martin-de-las Heras et al, 2000a).…”

“…This attribute was used as an indirect measure of MMPinduced hydrolysis of endogenous matrix collagen (Carrilho et al, 2009;Tezvergil-Mutluay et al, 2010). After incubation, the beams were transferred to individually labeled, uncapped polypropylene tubes and placed in a sealed desiccator containing anhydrous calcium sulfate (Drierite, W.A.…”