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Published on: July 10, 2014
A poly(2-hydroxyethyl methacrylate)-based resin improves the dentin remineralizing ability of calcium silicates
Paola Taddei1, Carlo Prati2, Maria Giovanna Gandolfi3
1Department of Biomedical and Neuromotor Sciences, Biochemistry Unit, University of Bologna, Via Belmeloro 8/2, 40126 Bologna, Italy.
Abstract:
Bioactive polymeric composites have received great attention for their capability to remineralize the dentin tissue. This study was aimed at evaluating if a poly(HEMA-co-TEGDMA) resin (HEMA: 2-hydroxyethyl methacrylate; TEGDMA: triethyleneglycol dimethacrylate) may increase the in vitro apatite forming ability of a calcium silicate cement (CaSi), in view of developing a hydrophilic light-curable composite bio-remineralizing restorative material (R-CaSi). To this purpose, the following experiments were carried out: (1) In vitro apatite forming ability of R-CaSi and CaSi was comparatively assessed by micro-Raman spectroscopy after immersion of the cement disks in Dulbecco's Phosphate Buffered Saline (DPBS) at 37°C for 1-28days; (2) Previously demineralized human dentin slices were soaked for 7days in close contact with the CaSi and R-CaSi cements as well as poly(HEMA), poly(TEGDMA) and poly(HEMA-co-TEGDMA), and then were comparatively analyzed by IR spectroscopy. Micro-Raman spectroscopy showed that in calcium phosphate nucleation tests, the B-type carbonated apatite deposit formed on R-CaSi was thicker than that on CaSi; therefore, the poly(HEMA-co-TEGDMA) resin proved able to increase the in vitro apatite forming ability of the calcium silicate-based cement. Both cements were found to induce dentin remineralization, R-CaSi to a higher extent, in agreement with the calcium phosphate nucleation tests. This result may be ascribed to the positive role played by the polymeric component, which was found to interact with collagen and to chelate calcium ions. Upon remineralization, collagen underwent conformational rearrangements and the formed apatite phase, rather than a simple deposit, was intimately bound to the collagen matrix, thanks to the calcium ions chelated by it.
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