Recombinant amelogenin peptide TRAP promoting remineralization of early enamel caries: An in vitro study

Objective: To explore the regulatory effect of recombinant amelogenin peptide TRAP on the remineralization of early enamel carious lesions.Methods: Forty-eight bovine enamel blocks that prepared initial lesions in vitro were split at random into four groups for immersion treatment for 12 days: 1) re...

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Main Authors: Yaru Li, Yiwei Li, Qinghua Bai, Mingzhu Wen, Dandan Ma, Yisha Lin, Jinpu Chu
Format: Article
Language:English
Published: Frontiers Media S.A. 2023-01-01
Series:Frontiers in Physiology
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fphys.2023.1076265/full
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author Yaru Li
Yaru Li
Yiwei Li
Yiwei Li
Qinghua Bai
Qinghua Bai
Mingzhu Wen
Mingzhu Wen
Dandan Ma
Yisha Lin
Yisha Lin
Jinpu Chu
author_facet Yaru Li
Yaru Li
Yiwei Li
Yiwei Li
Qinghua Bai
Qinghua Bai
Mingzhu Wen
Mingzhu Wen
Dandan Ma
Yisha Lin
Yisha Lin
Jinpu Chu
author_sort Yaru Li
collection DOAJ
description Objective: To explore the regulatory effect of recombinant amelogenin peptide TRAP on the remineralization of early enamel carious lesions.Methods: Forty-eight bovine enamel blocks that prepared initial lesions in vitro were split at random into four groups for immersion treatment for 12 days: 1) remineralizing medium; 2) studied peptide 1 (consisting of the N- and C-termini of porcine amelogenin) + remineralizing medium; 3) studied peptide 2 (TRAP) + remineralizing medium; 4) fluoride + remineralizing medium. After demineralization and remineralization immersion, each specimen’s mean mineral loss and lesion depth were measured using micro-computed tomography (micro-CT). The changes in lesion depth (∆LD) and mineral gain (∆Z) were computed following remineralization. The enamel samples were then cut into sections and examined with polarized light microscopy (PLM). The cross-section morphology was observed by scanning electron microscopy (SEM). The crystal phase was analyzed by an X-ray micro-diffractometer (XRD). The calcium-binding properties were determined using isothermal titration calorimetry (ITC).Results: Micro-CT analysis revealed a significant reduction in mineral loss in the four groups following the remineralization treatment (p < 0.05). The treatment with fluoride resulted in the greatest ∆Z and ∆LD, whereas the treatment with a remineralizing medium showed the least ∆Z and ∆LD among all groups. The ∆Z and ∆LD of the studied peptide 1 and studied peptide 2 groups were greater than those of the remineralizing medium group. However, there was no significant difference between the studied peptide 1 and studied peptide 2 groups (p > 0.05). All of the samples that the PLM analyzed had a thickening of the surface layer. A negative birefringent band changed in the lesion’s body. The SEM displayed that minerals were formed in all four groups of samples. The XRD results indicated that the products of remineralization of the studied peptide were hydroxyapatite crystals (HA). ITC showed that there were two binding modes between the calcium and peptide TRAP.Conclusion: This study confirmed the potential of the recombinant amelogenin peptide TRAP as a key functional motif of amelogenin protein for enamel remineralization and provided a promising biomaterial for remineralization in initial enamel carious lesion treatment.
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spelling doaj.art-bd2b1a70b45743ea97162b0caa93df102023-01-23T06:29:20ZengFrontiers Media S.A.Frontiers in Physiology1664-042X2023-01-011410.3389/fphys.2023.10762651076265Recombinant amelogenin peptide TRAP promoting remineralization of early enamel caries: An in vitro studyYaru Li0Yaru Li1Yiwei Li2Yiwei Li3Qinghua Bai4Qinghua Bai5Mingzhu Wen6Mingzhu Wen7Dandan Ma8Yisha Lin9Yisha Lin10Jinpu Chu11The First Affiliated Hospital of Zhengzhou University, Zhengzhou, ChinaCollege of Stomatology, Zhengzhou University, Zhengzhou, ChinaThe First Affiliated Hospital of Zhengzhou University, Zhengzhou, ChinaCollege of Stomatology, Zhengzhou University, Zhengzhou, ChinaThe First Affiliated Hospital of Zhengzhou University, Zhengzhou, ChinaCollege of Stomatology, Zhengzhou University, Zhengzhou, ChinaThe First Affiliated Hospital of Zhengzhou University, Zhengzhou, ChinaCollege of Stomatology, Zhengzhou University, Zhengzhou, ChinaThe First Affiliated Hospital of Zhengzhou University, Zhengzhou, ChinaThe First Affiliated Hospital of Zhengzhou University, Zhengzhou, ChinaCollege of Stomatology, Zhengzhou University, Zhengzhou, ChinaThe First Affiliated Hospital of Zhengzhou University, Zhengzhou, ChinaObjective: To explore the regulatory effect of recombinant amelogenin peptide TRAP on the remineralization of early enamel carious lesions.Methods: Forty-eight bovine enamel blocks that prepared initial lesions in vitro were split at random into four groups for immersion treatment for 12 days: 1) remineralizing medium; 2) studied peptide 1 (consisting of the N- and C-termini of porcine amelogenin) + remineralizing medium; 3) studied peptide 2 (TRAP) + remineralizing medium; 4) fluoride + remineralizing medium. After demineralization and remineralization immersion, each specimen’s mean mineral loss and lesion depth were measured using micro-computed tomography (micro-CT). The changes in lesion depth (∆LD) and mineral gain (∆Z) were computed following remineralization. The enamel samples were then cut into sections and examined with polarized light microscopy (PLM). The cross-section morphology was observed by scanning electron microscopy (SEM). The crystal phase was analyzed by an X-ray micro-diffractometer (XRD). The calcium-binding properties were determined using isothermal titration calorimetry (ITC).Results: Micro-CT analysis revealed a significant reduction in mineral loss in the four groups following the remineralization treatment (p < 0.05). The treatment with fluoride resulted in the greatest ∆Z and ∆LD, whereas the treatment with a remineralizing medium showed the least ∆Z and ∆LD among all groups. The ∆Z and ∆LD of the studied peptide 1 and studied peptide 2 groups were greater than those of the remineralizing medium group. However, there was no significant difference between the studied peptide 1 and studied peptide 2 groups (p > 0.05). All of the samples that the PLM analyzed had a thickening of the surface layer. A negative birefringent band changed in the lesion’s body. The SEM displayed that minerals were formed in all four groups of samples. The XRD results indicated that the products of remineralization of the studied peptide were hydroxyapatite crystals (HA). ITC showed that there were two binding modes between the calcium and peptide TRAP.Conclusion: This study confirmed the potential of the recombinant amelogenin peptide TRAP as a key functional motif of amelogenin protein for enamel remineralization and provided a promising biomaterial for remineralization in initial enamel carious lesion treatment.https://www.frontiersin.org/articles/10.3389/fphys.2023.1076265/fullpeptide TRAPenamel cariesremineralizationamelogeninmicro-CT
spellingShingle Yaru Li
Yaru Li
Yiwei Li
Yiwei Li
Qinghua Bai
Qinghua Bai
Mingzhu Wen
Mingzhu Wen
Dandan Ma
Yisha Lin
Yisha Lin
Jinpu Chu
Recombinant amelogenin peptide TRAP promoting remineralization of early enamel caries: An in vitro study
Frontiers in Physiology
peptide TRAP
enamel caries
remineralization
amelogenin
micro-CT
title Recombinant amelogenin peptide TRAP promoting remineralization of early enamel caries: An in vitro study
title_full Recombinant amelogenin peptide TRAP promoting remineralization of early enamel caries: An in vitro study
title_fullStr Recombinant amelogenin peptide TRAP promoting remineralization of early enamel caries: An in vitro study
title_full_unstemmed Recombinant amelogenin peptide TRAP promoting remineralization of early enamel caries: An in vitro study
title_short Recombinant amelogenin peptide TRAP promoting remineralization of early enamel caries: An in vitro study
title_sort recombinant amelogenin peptide trap promoting remineralization of early enamel caries an in vitro study
topic peptide TRAP
enamel caries
remineralization
amelogenin
micro-CT
url https://www.frontiersin.org/articles/10.3389/fphys.2023.1076265/full
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