Mimicking amelogenesis to remineralize enamel through co-assembly of PTL fibrils and CMC/ACP
Enamel remineralization has important clinical value for the prevention and minimally invasive treatment of early enamel caries. Enamel matrix proteins (EMPs) are believed to play a key role in amelogenesis to regulate the growth and organization of enamel. Three “key events” of amelogenesis indicat...
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| Format: | Article |
| Language: | English |
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Elsevier
2023-02-01
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| Series: | Materials & Design |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S0264127523000692 |
| _version_ | 1811158435469721600 |
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| author | Yangyang Ye Runqiu Lu Hao Ren Yang Yang Tianqi Li Xiangyu Zhang Peng Yang Xu Zhang |
| author_facet | Yangyang Ye Runqiu Lu Hao Ren Yang Yang Tianqi Li Xiangyu Zhang Peng Yang Xu Zhang |
| author_sort | Yangyang Ye |
| collection | DOAJ |
| description | Enamel remineralization has important clinical value for the prevention and minimally invasive treatment of early enamel caries. Enamel matrix proteins (EMPs) are believed to play a key role in amelogenesis to regulate the growth and organization of enamel. Three “key events” of amelogenesis indicated the co-assembly of EMPs composed of amyloid amelogenin (templating protein) and non-amelogenin (non-templating protein) with amorphous calcium phosphate (ACP), followed by the transformation into the crystalline phase with the help of proteolytic enzymes. Herein, a biomimetic microenvironment is constructed, adhesive phase-transited lysozyme fibrils (PTL fibrils) mimicking amelogenin template through amyloid-like lysozyme aggregation, acid carboxymethyl chitosan (CMC) and sodium hypochlorite (NaClO) mimicking non-amelogenin and proteolytic enzymes, respectively. Based on the synchronous self-assembly and mineralization, the full process of the three “key events” of biomineralization were reverted in vitro by slowly raising the pH of the system through dialysis, in-situ regenerating enamel-like crystals with properly oriented structure and mechanical properties that are close to natural enamel independent of additional mineral ions. Especially, the present study proposed the crucial role of the amyloid conformation transition of amelogenin and supported a promising biomimetic strategy for enamel repair. |
| first_indexed | 2024-04-10T05:24:39Z |
| format | Article |
| id | doaj.art-51da896727e84b4788a8a999de320b2b |
| institution | Directory Open Access Journal |
| issn | 0264-1275 |
| language | English |
| last_indexed | 2024-04-10T05:24:39Z |
| publishDate | 2023-02-01 |
| publisher | Elsevier |
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| series | Materials & Design |
| spelling | doaj.art-51da896727e84b4788a8a999de320b2b2023-03-08T04:13:44ZengElsevierMaterials & Design0264-12752023-02-01226111654Mimicking amelogenesis to remineralize enamel through co-assembly of PTL fibrils and CMC/ACPYangyang Ye0Runqiu Lu1Hao Ren2Yang Yang3Tianqi Li4Xiangyu Zhang5Peng Yang6Xu Zhang7School and Hospital of Stomatology, Tianjin Medical University, Tianjin 300070, ChinaKey Laboratory of Applied Surface and Colloid Chemistry Ministry of Education School of Chemistry and Chemical Engineering, Shaanxi Normal University, Xi’an 710119, ChinaKey Laboratory of Applied Surface and Colloid Chemistry Ministry of Education School of Chemistry and Chemical Engineering, Shaanxi Normal University, Xi’an 710119, ChinaInstitute of Applied Chemistry and Engineering, College of Chemistry, Nankai University, Tianjin 300071, ChinaSchool and Hospital of Stomatology, Tianjin Medical University, Tianjin 300070, ChinaDepartment of Pediatric Dentistry, School and Hospital of Stomatology, Tianjin Medical University, Tianjin 300070, China; Corresponding authors at: School of Stomatology, Hospital of Stomatology, Tianjin Medical University, Tianjin 300070, China.Key Laboratory of Applied Surface and Colloid Chemistry Ministry of Education School of Chemistry and Chemical Engineering, Shaanxi Normal University, Xi’an 710119, China; Corresponding authors at: School of Stomatology, Hospital of Stomatology, Tianjin Medical University, Tianjin 300070, China.School and Hospital of Stomatology, Tianjin Medical University, Tianjin 300070, China; Institute of Stomatology, Tianjin Medical University, Tianjin 300070, China; Corresponding authors at: School of Stomatology, Hospital of Stomatology, Tianjin Medical University, Tianjin 300070, China.Enamel remineralization has important clinical value for the prevention and minimally invasive treatment of early enamel caries. Enamel matrix proteins (EMPs) are believed to play a key role in amelogenesis to regulate the growth and organization of enamel. Three “key events” of amelogenesis indicated the co-assembly of EMPs composed of amyloid amelogenin (templating protein) and non-amelogenin (non-templating protein) with amorphous calcium phosphate (ACP), followed by the transformation into the crystalline phase with the help of proteolytic enzymes. Herein, a biomimetic microenvironment is constructed, adhesive phase-transited lysozyme fibrils (PTL fibrils) mimicking amelogenin template through amyloid-like lysozyme aggregation, acid carboxymethyl chitosan (CMC) and sodium hypochlorite (NaClO) mimicking non-amelogenin and proteolytic enzymes, respectively. Based on the synchronous self-assembly and mineralization, the full process of the three “key events” of biomineralization were reverted in vitro by slowly raising the pH of the system through dialysis, in-situ regenerating enamel-like crystals with properly oriented structure and mechanical properties that are close to natural enamel independent of additional mineral ions. Especially, the present study proposed the crucial role of the amyloid conformation transition of amelogenin and supported a promising biomimetic strategy for enamel repair.http://www.sciencedirect.com/science/article/pii/S0264127523000692Biomimetic mineralizationEnamelAmorphous calcium phosphateAmelogeninSynchronous self-assembly and mineralization |
| spellingShingle | Yangyang Ye Runqiu Lu Hao Ren Yang Yang Tianqi Li Xiangyu Zhang Peng Yang Xu Zhang Mimicking amelogenesis to remineralize enamel through co-assembly of PTL fibrils and CMC/ACP Materials & Design Biomimetic mineralization Enamel Amorphous calcium phosphate Amelogenin Synchronous self-assembly and mineralization |
| title | Mimicking amelogenesis to remineralize enamel through co-assembly of PTL fibrils and CMC/ACP |
| title_full | Mimicking amelogenesis to remineralize enamel through co-assembly of PTL fibrils and CMC/ACP |
| title_fullStr | Mimicking amelogenesis to remineralize enamel through co-assembly of PTL fibrils and CMC/ACP |
| title_full_unstemmed | Mimicking amelogenesis to remineralize enamel through co-assembly of PTL fibrils and CMC/ACP |
| title_short | Mimicking amelogenesis to remineralize enamel through co-assembly of PTL fibrils and CMC/ACP |
| title_sort | mimicking amelogenesis to remineralize enamel through co assembly of ptl fibrils and cmc acp |
| topic | Biomimetic mineralization Enamel Amorphous calcium phosphate Amelogenin Synchronous self-assembly and mineralization |
| url | http://www.sciencedirect.com/science/article/pii/S0264127523000692 |
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