Dentin is a complex composite of organized collagen matrix filled with submicron-sized calcium-deficient, carbonate-rich apatite crystallites. Together, the collagen and apatites form dentinal tubules that house the odontoblasts. Unlike enamel, exposed dentin can result in hypersensitivity which is often treated with desensitizing toothpastes which are not always effective, necessitating the placement of artificial restorative materials if the hypersensitivity persists. A preferred approach is to promote the deposition of apatite like minerals onto exposed dentin surfaces. Dentin phosphoprotein (DPP) is known to play a critical role in tooth mineralization and is the most abundant non-collagenous extracellular matrix component in dentin. DPP contains high concentrations of serine (45-50 %) and aspartic acid (35-38 %), and human DPP contains numerous repetitive nucleotide sequences of aspartate-serine-serine (DSS) that promote the formation of hydroxyapatite. Of these, the octuple repeats of aspartate-serine-serine, DSS-8 peptides, are the most active in the mediation of biologically directed mineral deposition. This study investigates the effects of DSS-8 on microstructures, phase composition, hardness and elastic modulus for human dentin in the remineralization process.
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