Abstract
This in vitro study aimed to accelerate the remineralization of a completely demineralized dentine collagen block in order to regenerate the dentinal microstructure of calcified collagen fibrils by a novel electric field-aided biomimetic mineralization system in the absence of non-collagenous proteins. Completely demineralized human dentine slices were prepared using ethylene diamine tetraacetic acid (EDTA) and treated with guanidine hydrochloride to extract the bound non-collagenous proteins. The completely demineralized dentine collagen blocks were then remineralized in a calcium chloride agarose hydrogel and a sodium hydrogen phosphate and fluoride agarose hydrogel. This process was accelerated by subjecting the hydrogels to electrophoresis at 20 mA for 4 and 12 h. X-ray diffraction (XRD), scanning electron microscopy (SEM), energy dispersive X-ray spectroscopy (EDX), and transmission electron microscopy (TEM) were used to evaluate the resultant calcification of the dentin collagen matrix. SEM indicated that mineral particles were precipitated on the intertubular dentin collagen matrix; these densely packed crystals mimicked the structure of the original mineralized dentin. However, the dentinal tubules were not occluded by the mineral crystals. XRD and EDX both confirmed that the deposited crystals were fluorinated hydroxyapatite. TEM revealed the existence of intrafibrillar and interfibrillar mineralization of the collagen fibrils. A novel electric field-aided biomimetic mineralization system was successfully developed to remineralize a completely demineralized dentine collagen matrix in the absence of non-collagenous proteins. This study developed an accelerated biomimetic mineralization system which can be a potential protocol for the biomineralization of dentinal defects.
Highlights
Dentin is the main component of teeth
The classical ion-based crystallization concept may not be applicable for remineralizing completely demineralized dentin [3]. Several approaches, such as those using supersaturated calcium phosphate solution, bioactive glass particles [4], polydopamine [5], calcium phosphate-loaded gel [6], and casein phosphopeptide-amorphous calcium phosphate (CPP-ACP) [7], that could only induce HA to deposit on the dentin surface, which were not representative of the real remineralization of dentin collagen fibrils
The biomimicry of non-collagenous proteins (NCPs)-using substances such as polyacrylic acid (PAA), polyvinylphosphonic acid (PVPA) [8], sodium trimetaphosphate (STMP) [9], oligopeptides inspired by NCPs [10], polymer-induced liquid precursors that use poly-L-aspartate sodium salt to stabilize a precursor phase of amorphous calcium phosphate (ACP) [11], and poly(amidoamine) dendrimers [12], have been shown to remineralize the dentin collagen matrix by duplicating the dentin microstructure within calcified collagen fibrils
Summary
Dentin is the main component of teeth. Structurally, the basic microstructure of dentin is composed of a calcified collagen matrix, which is made up of inorganic hydroxyapatite (HA) based minerals (approximately 70% by weight), organic matrix (20%), and water (10%). The advantages of using a completely demineralized dentin collagen matrix block include the elimination of the ambiguity that arises when trying to discern the remineralized apatite crystallites from the remnant apatite seed crystallites and the ability to ascertain whether the remineralization of collagen matrix can occur in the absence of NCPs. In a previous study, we developed a technique to remineralize dentin collagen fibrils in partially demineralized dentin slices using the aid of electrophoresis [14]. We hypothesized that this powerful technique could remineralize a completely demineralized dentin collagen matrix block and aimed to both regenerate the tooth microstructure and to shorten the mineralization time
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