DOI: 10.3290/j.jad.a9506Pages 175-182, Language: EnglishMountouris, George/Silikas, Nick/Eliades, GeorgeThe aim of the present study was to evaluate the deproteination potential of 5% aqueous NaOCl solution applied by rubbing action on the molecular composition and morphology of smear-layer covered and acid-etched human coronal dentin surfaces.
Paired specimens (n = 4 x 2 per group) of acid-etched (Group A) and smear-layer covered (Group B) human coronal dentin surfaces were sequentially treated with the NaOCl solution for time intervals ranging from 5 s to 120 s and analyzed by reflectance FTIR microspectroscopy and tapping mode atomic force microscopy. The changes in the mineral (v4 P-O stretching vibrations) to matrix (C = O stretching vibrations of amide I) peak area ratios and in the Ra roughness parameter were used to quantify the effect of treatment. Two-way ANOVA and Dunn's tests were used to assess the differences within each group and between groups (a = 0.05).
In both groups, NaOCl treatment reduced organic matrix (amide I, II, III peaks), but did not affect carbonates and phosphates. In group A, the rate of deproteination was slow, and reached a peak value after 120 s. Tubule orifices became visible after 40 s of treatment; after 120 s, excessive porosity was detected, with Ra values presenting no statistically significant difference from group B. In group B after 10 s, the extent of deproteination was enhanced, reaching a plateau between 30 s and 60 s, and attaining a maximum after 120 s. Tubule diameter, intertubular porosity, and Ra were increased; intertubular dentin area was reduced. For both groups after 40 s of treatment, the mineral to matrix ratio recorded was similar to smear-layer-free sectioned dentin.
The results of the present study imply that deproteination of mineralized or acid-etched dentin surfaces within a clinically relevant time frame may provide methods for bonding to dentin alternative to conventional technique-sensitive dentin hybridization.
Keywords: dentin, sodium hypochlorite, FTIR, AFM, deproteination