Background: The tyrosine-rich amelogenin peptide (TRAP) is the main enzymatic hydrolysis product of amelogenin during enamel development. The TRAP peptide has been shown to promote the remineralization of early enamel caries in vitro. The aim of this crossover blinded and randomized study was to evaluate the impact of recombinant amelogenin peptide TRAP on the remineralization of initial enamel caries lesions in situ.
Methods: The binding capacity of recombinant amelogenin peptide TRAP to hydroxyapatite (HA) and a demineralized enamel surface was analyzed by a Langmuir adsorption isotherm experiment and confocal laser scanning microscopy (CLSM). Subsequently, the remineralization effect of recombinant amelogenin peptide TRAP on initial enamel carious lesions was studied using an in situ caries model. In this randomized, crossover, and blinded study, 12 volunteers wearing intraoral removable in-situ appliances with one bovine enamel block were divided into three groups: Group A received deionized water (DDW, negative control); Group B received recombinant amelogenin peptide TRAP (100 µg/ml); Group C received sodium fluoride (2 ppm). The study took place over three periods of 14 days each. At the end of each treatment period, the percentage of surface microhardness recovery (%SHR) and the integrated change in subsurface hardness (%ΔIHC) were evaluated.
Results: Recombinant amelogenin peptide TRAP adsorbed onto HA and demineralized enamel surfaces. After in situ analysis, all samples hardened significantly compared with baseline. Fluoride had a significantly greater effect than all other treatments. %SMHR was significantly greater than the DDW for the recombinant amelogenin peptide TRAP. Considering subsurface remineralization, treatment with recombinant amelogenin peptide TRAP and fluoride promoted increases of 6.73% and 15.68%, respectively, in %ΔIHC compared with DDW.
Conclusion: Recombinant amelogenin peptide TRAP can promote the remineralization of early enamel caries lesions in situ.
Clinical Relevance: This study demonstrated the potential of recombinant amelogenin peptide TRAP to assist in the remineralization of artificial carious lesions in situ. The amelogenin peptide TRAP may be a promising, non-fluorinated, biomimetic, remineralization anti-caries agent.
Clinical Trial Number: Not applicable.
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http://dx.doi.org/10.1186/s12903-025-05643-w | DOI Listing |
BMC Oral Health
February 2025
The First Affiliated Hospital of Zhengzhou University, Zhengzhou, China.
Background: The tyrosine-rich amelogenin peptide (TRAP) is the main enzymatic hydrolysis product of amelogenin during enamel development. The TRAP peptide has been shown to promote the remineralization of early enamel caries in vitro. The aim of this crossover blinded and randomized study was to evaluate the impact of recombinant amelogenin peptide TRAP on the remineralization of initial enamel caries lesions in situ.
View Article and Find Full Text PDFBiomimetics (Basel)
February 2025
Center for Craniofacial Molecular Biology, Herman Ostrow School of Dentistry, University of Southern California, Los Angeles, CA 90089, USA.
Peptide-based biomimetic treatments have gained increased attention in the dental field due to their biocompatibility and minimally invasive qualities. These biomimetic approaches can replicate the native architecture of dental tissues, thus contributing to higher success rates and improved longevity of restorations. The aim of this study was first to examine the biocompatibility and stability of an amelogenin peptide-based chitosan hydrogel (P26-CS) against salivary enzymes.
View Article and Find Full Text PDFGels
December 2024
Faculty of Medicine and Pharmacy, University of Oradea, P-ta 1 Decembrie 10, 410087 Oradea, Romania.
This study investigates the microstructure of dental enamel following demineralization and re-mineralization processes, using DIAGNOdent scores and images obtained via scanning electron microscopy (SEM), atomic force microscopy (AFM), and microhardness (Vickers). The research evaluates the effects of two experimental hydrogels, Anti-Amelogenin isoform X (ABT260, S1) and Anti-Kallikrein L1 (K3014, S2), applied to demineralized enamel surfaces over periods of 14 and 21 days. The study involved 60 extracted teeth, free from cavities or other lesions, divided into four groups: a positive group (+), a negative group (-) and groups S1 and S2.
View Article and Find Full Text PDFACS Appl Mater Interfaces
January 2025
Department of Cariology and Endodontology, Peking University School and Hospital of Stomatology & National Center for Stomatology & National Clinical Research Center for Oral Diseases & National Engineering Research Center of Oral Biomaterials and Digital Medical Devices & Beijing Key Laboratory of Digital Stomatology & NHC Key Laboratory of Digital Stomatology & NMPA Key Laboratory for Dental Materials, Beijing 100081, China.
J Pharm Biomed Anal
March 2025
Department of Chemistry, University of Reading, Whiteknights, Reading RG6 6DX, United Kingdom. Electronic address:
The biological sex estimation of human individuals can be achieved by extracting fragments of the amelogenin protein from small areas of tooth enamel. The amelogenin gene can be found on both sex chromosomes (X and Y) with chromosome-specific differences in its sequence, and consequently the sequences of the expressed protein in teeth. Virtually all current analytical techniques used to identify the occurrence of the male Y chromosome-specific proteoform employ proteoform-specific peptide analysis by LC-ESI MS/MS, which typically results in longer analytical times due to the LC separation step, despite recent efforts of shortening the LC step.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!