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      Remineralization Efficacy of an Amelogenin-Based Synthetic Peptide on Carious Lesions

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          Abstract

          Objective: The aim of this study was to evaluate the remineralization efficacy of an amelogenin-based peptide on initial enamel carious lesions in vitro. Furthermore, we attempted to provide insights into the possible mechanism of the remineralization, including determining the calcium-binding properties of the peptide and its effects on calcium phosphate mineralization.

          Methods: The peptide comprising the N-terminus and the C-terminus of porcine amelogenin was synthesized by Synpeptide Co., Ltd. Fifty specimens were randomly assigned to five immersing treatment groups for 12 days: remineralizing medium only; 12.5 μg/mL peptide + remineralizing medium; 25 μg/mL peptide + remineralizing medium; 50 μg/mL peptide + remineralizing medium; fluoride + remineralizing medium. After immersion, mean mineral loss before and after remineralization of each specimen was determined using micro-CT. Mean mineral gain after remineralization was calculated. Calcium binding properties were measured by Isothermal titration calorimetry (ITC). TEM and Fourier transform-infrared were used to determine the effects of the peptide on calcium phosphate mineralization.

          Results: A significant decrease in mineral loss after remineralization process in all groups was observed ( p < 0.05). Treatment in remineralizing medium resulted in the lowest mineral gain while the fluoridated treatment exhibited the highest mineral gain among all groups. Inclusion of synthetic peptide in the remineralizing medium exhibited a higher mineral gain and the gain of 50 μg/mL group was greater than that of the 25 μg/mL group. No significant difference in mineral gain was observed between the remineralizing medium only group and the 12.5 μg/mL peptide group ( p > 0.05). ITC values showed that the Ca 2+-binding affinity of the peptide is about 9.914 × 10 4M −1. Furthermore, the peptide was found to inhibit calcium phosphate precipitation and stabilize amorphous calcium phosphate formation for more than 2 h and finally transform into ordered hydroxyapatite crystals.

          Conclusion: Specific concentrations of the amelogenin-based synthetic peptide promoted in vitro remineralization, with higher concentrations exhibiting significantly greater remineralization. This study presented evidence suggesting that the peptide may act as a Ca 2+carrier as well as a regulating factor. When the stabilizing calcium and phosphorus ions bind with the peptide they become biologically available for the remineralization of deeper carious lesions, while also regulated by the peptide to transform into ordered hydroxyapatite crystals.

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          Amorphous calcium phosphate is a major component of the forming fin bones of zebrafish: Indications for an amorphous precursor phase.

          A fundamental question in biomineralization is the nature of the first-formed mineral phase. In vertebrate bone formation, this issue has been the subject of a long-standing controversy. We address this key issue using the continuously growing fin bony rays of the Tuebingen long-fin zebrafish as a model for bone mineralization. Employing high-resolution scanning and transmission electron microscopy imaging, electron diffraction, and elemental analysis, we demonstrate the presence of an abundant amorphous calcium phosphate phase in the newly formed fin bones. The extracted amorphous mineral particles crystallize with time, and mineral crystallinity increases during bone maturation. Based on these findings, we propose that this amorphous calcium phosphate phase may be a precursor phase that later transforms into the mature crystalline mineral.
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            The structural biology of the developing dental enamel matrix.

            The biomineralization of the dental enamel matrix with a carbonated hydroxyapatite mineral generates one of the most remarkable examples of a vertebrate mineralized tissue. Recent advances in the molecular biology of ameloblast gene products have now revealed the primary structures of the principal proteins involved in this extracellular mineralizing system, amelogenins, tuftelins, ameloblastins, enamelins, and proteinases, but details of their secondary, tertiary, and quaternary structures, their interactions with other matrix and or cell surface proteins, and their functional role in dental enamel matrix mineralization are still largely unknown. This paper reviews our current knowledge of these molecules, the probable molecular structure of the enamel matrix, and the functional role of these extracellular matrix proteins. Recent studies on the major structural role played by the amelogenin proteins are discussed, and some new data on synthetic amelogenin matrices are reviewed. Copyright 1999 Academic Press.
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              Fluoride and casein phosphopeptide-amorphous calcium phosphate.

              Casein phosphopeptide-amorphous calcium phosphate (CPP-ACP) slows the progression of caries and remineralizes enamel subsurface lesions. The aim of this study was to determine the ability of CPP-ACP to increase the incorporation of fluoride into plaque and to promote enamel remineralization in situ. Randomized, double-blind, cross-over studies involved mouthrinses and dentifrices containing CPP-ACP and fluoride. The mouthrinses were used for 60 sec, three times/day for 5 days, and supragingival plaque was collected and analyzed for F. The dentifrices were rinsed as a water slurry for 60 sec four times/day for 14 days in an in situ model. The addition of 2% CPP-ACP to the 450-ppm-F mouthrinse significantly increased the incorporation of fluoride into plaque. The dentifrice containing 2% CPP-ACP produced a level of remineralization similar to that achieved with a dentifrice containing 2800 ppm F. The dentifrice containing 2% CPP-ACP plus 1100 ppm F was superior to all other formulations.
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                Author and article information

                Contributors
                Journal
                Front Physiol
                Front Physiol
                Front. Physiol.
                Frontiers in Physiology
                Frontiers Media S.A.
                1664-042X
                05 July 2018
                2018
                : 9
                : 842
                Affiliations
                [1] 1The First Affiliated Hospital of Zhengzhou University , Zhengzhou, China
                [2] 2College of Stomatology, Zhengzhou University , Zhengzhou, China
                Author notes

                Edited by: Udo Jochen Birk, Johannes Gutenberg-Universität Mainz, Germany

                Reviewed by: Michel Goldberg, Institut National de la Santé et de la Recherche Médicale (INSERM), France; Alexandre Rezende Vieira, University of Pittsburgh, United States

                These authors have contributed equally to this work.

                This article was submitted to Biomedical Physics, a section of the journal Frontiers in Physiology

                Article
                10.3389/fphys.2018.00842
                6041723
                30026702
                8c1f85c0-060f-40f2-83af-dfcb65b8d112
                Copyright © 2018 Chu, Feng, Guo, Zhang, Zhao and Zhang.

                This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

                History
                : 10 January 2018
                : 14 June 2018
                Page count
                Figures: 8, Tables: 1, Equations: 1, References: 52, Pages: 11, Words: 0
                Funding
                Funded by: Natural Science Foundation of Henan Province 10.13039/501100006407
                Award ID: 162300410264
                Categories
                Physiology
                Original Research

                Anatomy & Physiology
                amelogenin-based synthetic peptide,early enamel lesion,biomimetic,remineralization,amorphous calcium phosphate

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