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- Publisher Website: 10.1007/s00784-013-1035-y
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- PMID: 23912147
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Article: A novel oligopeptide simulating dentine matrix protein 1 for biomimetic mineralization of dentine
Title | A novel oligopeptide simulating dentine matrix protein 1 for biomimetic mineralization of dentine |
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Authors | |
Keywords | Biomimetic remineralization Biomineralization Collagen Dentine matrix protein Hydroxyapatite Oligopeptide |
Issue Date | 2014 |
Publisher | Springer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00784/index.htm |
Citation | Clinical Oral Investigations, 2014, v. 18 n. 3, p. 873-881 How to Cite? |
Abstract | Objective The objectives were to design and fabricate an oligopeptide that simulates dentine matrix protein 1 (DMP1) to study its ability to bind to dentine collagen fibrils and induce biomimetic mineralization for the management of dentine hypersensitivity. Materials and methods A novel oligopeptide was developed by connecting the collagen-binding domain of DMP1 to the hydrophilic C-terminal of amelogenin. Fluorescein isothiocyanate-coupled oligopeptide was applied to the completely demineralized dentine collagen and examined using fluorescent microscopy. The nucleation and growth of hydroxyapatite were initiated by immersing oligopeptide into calcium chloride and sodium hydrogen phosphate solutions. Scanning electron microscopy (SEM), transmission electron microscopy, and selected area electron diffraction (SAED) were used to examine the formation. Dentine slices were acid-etched, coated with oligopeptide, and immersed into a metastable calcium phosphate solution. Dentine mineralization was evaluated by SEM, X-ray diffraction (XRD), and Fourier transform infrared spectroscopy (FTIR). Results Fluorescent dentine collagen was identified in the specimens. The nucleation and growth of crystals were detected after immersing the oligopeptide into calcium chloride and sodium hydrogen phosphate solutions. Under SEM, crystals were observed covering the oligopeptide-coated dentine surface, within the demineralized dentine collagen matrix and occluding dentinal tubules. SAED, XRD, and FTIR confirmed that the crystals were hydroxyapatite. Conclusion A novel oligopeptide-simulating DMP1 was developed, that can bind to collagen fibrils, initiate mineralization, and induce biomimetic mineralization of dentine. Clinical relevance Biomimetic mineralization of dentine facilitated by this oligopeptide is a potential therapeutic technique for the management of dentine hypersensitivity. |
Persistent Identifier | http://hdl.handle.net/10722/192319 |
ISSN | 2023 Impact Factor: 3.1 2023 SCImago Journal Rankings: 0.942 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Cao, Y | en_US |
dc.contributor.author | Liu, W | en_US |
dc.contributor.author | Ning, T | en_US |
dc.contributor.author | Mei, ML | en_US |
dc.contributor.author | Li, Q-L | en_US |
dc.contributor.author | Lo, ECM | en_US |
dc.contributor.author | Chu, CH | en_US |
dc.date.accessioned | 2013-10-24T01:49:29Z | - |
dc.date.available | 2013-10-24T01:49:29Z | - |
dc.date.issued | 2014 | en_US |
dc.identifier.citation | Clinical Oral Investigations, 2014, v. 18 n. 3, p. 873-881 | en_US |
dc.identifier.issn | 1432-6981 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/192319 | - |
dc.description.abstract | Objective The objectives were to design and fabricate an oligopeptide that simulates dentine matrix protein 1 (DMP1) to study its ability to bind to dentine collagen fibrils and induce biomimetic mineralization for the management of dentine hypersensitivity. Materials and methods A novel oligopeptide was developed by connecting the collagen-binding domain of DMP1 to the hydrophilic C-terminal of amelogenin. Fluorescein isothiocyanate-coupled oligopeptide was applied to the completely demineralized dentine collagen and examined using fluorescent microscopy. The nucleation and growth of hydroxyapatite were initiated by immersing oligopeptide into calcium chloride and sodium hydrogen phosphate solutions. Scanning electron microscopy (SEM), transmission electron microscopy, and selected area electron diffraction (SAED) were used to examine the formation. Dentine slices were acid-etched, coated with oligopeptide, and immersed into a metastable calcium phosphate solution. Dentine mineralization was evaluated by SEM, X-ray diffraction (XRD), and Fourier transform infrared spectroscopy (FTIR). Results Fluorescent dentine collagen was identified in the specimens. The nucleation and growth of crystals were detected after immersing the oligopeptide into calcium chloride and sodium hydrogen phosphate solutions. Under SEM, crystals were observed covering the oligopeptide-coated dentine surface, within the demineralized dentine collagen matrix and occluding dentinal tubules. SAED, XRD, and FTIR confirmed that the crystals were hydroxyapatite. Conclusion A novel oligopeptide-simulating DMP1 was developed, that can bind to collagen fibrils, initiate mineralization, and induce biomimetic mineralization of dentine. Clinical relevance Biomimetic mineralization of dentine facilitated by this oligopeptide is a potential therapeutic technique for the management of dentine hypersensitivity. | - |
dc.language | eng | en_US |
dc.publisher | Springer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00784/index.htm | - |
dc.relation.ispartof | Clinical Oral Investigations | en_US |
dc.rights | This is a post-peer-review, pre-copyedit version of an article published in Clinical Oral Investigations. The final authenticated version is available online at: https://doi.org/10.1007/s00784-013-1035-y | - |
dc.subject | Biomimetic remineralization | - |
dc.subject | Biomineralization | - |
dc.subject | Collagen | - |
dc.subject | Dentine matrix protein | - |
dc.subject | Hydroxyapatite | - |
dc.subject | Oligopeptide | - |
dc.title | A novel oligopeptide simulating dentine matrix protein 1 for biomimetic mineralization of dentine | en_US |
dc.type | Article | en_US |
dc.description.nature | postprint | - |
dc.identifier.doi | 10.1007/s00784-013-1035-y | en_US |
dc.identifier.pmid | 23912147 | - |
dc.identifier.scopus | eid_2-s2.0-84897574563 | en_US |
dc.identifier.hkuros | 226787 | - |
dc.identifier.hkuros | 228337 | - |
dc.identifier.hkuros | 238337 | - |
dc.identifier.hkuros | 231334 | - |
dc.identifier.spage | 873 | en_US |
dc.identifier.epage | 881 | en_US |
dc.identifier.isi | WOS:000333799600023 | - |
dc.publisher.place | Germany | - |
dc.identifier.issnl | 1432-6981 | - |