Biomimetic Mineralization for Enamel and Dentin: Comparison
View Latest Version
Please note this is a comparison between Version 2 by Catherine Yang and Version 1 by Changyu Shao.

The tooth, including enamel and dentin, is a prominent biomineral that is produced by the biomineralization of living organisms. In clinical dentistry, traditional remineralization is achieved by using fluoride to enhance the deposition of calcium phosphate on the enamel surface, which is called an acid-resistant layer of fluorapatite. Despite this method having been successful in hardening enamel, the structure of this mineral layer is disordered and loose, and distinct from the natural enamel. Inspired by the process of natural enamel formation, strategies of biomimetic remineralization have been proposed and developed for several decades. These strategies include simulating in-body mineralization conditions, such as the enamel disks immersed in simulated body fluid, to mimic the function of the proteins involved in the biomineralization of the tooth, and constructing a mineralization front similar to that observed during the formation of calcified tissue. These methods allow the regrowth of HAP crystals on the enamel surface in an attempt to replicate the complex structure of the tooth and restore its mechanical properties.

  • biomimetic mineralization
  • tooth
  • enamel
  • dentin
  • hydroxyapatite

1. Enamel Remineralization

1.1. Amelogenin and Amelogenin-Inspired Peptides

Amelogenin, the major protein associated with enamel formation, is secreted by the ameloblasts and accounts for 80%–90% of the proteins in the developing enamel matrix. It consists of 178 amino acids and is rich in proline, glutamic acid, histidine, and leucine. Amelogenin is a hydrophobic macromolecule, but it contains a series of hydrophilic amino acid residues at its C-terminus. In an aqueous solution, the adjustment of the pH and ion strength of the solution can induce amelogenin molecules to assemble into nanospheres [60,61][1][2], with a hydrophobic center and a hydrophilic surface. These nanospheres can further self-assemble to form microfibers [62][3]. These amelogenin assemblies play a key role in controlling crystal orientation and crystal-oriented growth during the enamel formation [63][4].
Since the synthesis process of amelogenin and MMP-20 is complex and costly, amelogenin-based peptides are utilized in the biomimetic mineralization of enamel. Ren et al. added hydrophilic segments (TKREEVD) to five Gln-Pro-X repeat sequences (QPYQPVQPHQPMQPQ) to form an enamel protein-derived peptide (QP5). QP5 can promote the long-term remineralization of early dental caries [54][5]. Ding et al. reported that the combined use of fluoride and QP5 has a potential synergistic effect on the remineralization of dental caries, and the microhardness of the repair layer is significantly improved [65][6]. However, the shape, size, and orientation of the mineralized layer crystals exhibit notable differences compared to natural enamel. Further research into the logic and efficacy of peptide design is of considerable importance.
Due to the difficulty of obtaining amelogenin, there are significant limitations to its research and application. Currently, a synthetic protein polyamidoamine-amine-type dendrimer (PAMAM) can be successfully prepared and applied to the repair of the enamel. This kind of dendritic molecule can self-assemble into spherical macromolecules in solution and then convert into linear macromolecules, a behavior similar to that of amelogenin [67,68][7][8]. These artificial proteins are adsorbed on the enamel surface and further self-assembled, and then induce the deposition of calcium and phosphorus in the solution to achieve ordered growth. However, there is still a significant gap compared to natural enamel, and in these experiments, the repair effect is better with the synergistic participation of fluoride ions than with PAMAM polymers alone.

1.2. Calcium Phosphate Particle-Based Systems

Investigations into nature have shown that the growth of the zebrafish skeleton involves an integral compound known as amorphous calcium phosphate (ACP) [71][9]. This intermediate, amorphous substance plays a pivotal role in the formation of these integral minerals [72][10]. In addition, ACP is the initial deposition mineral in the early stages of enamel biogenesis [73,74][11][12].
In an attempt to mimic the biomineralization process, a variety of composite materials containing ACP nanoparticles have been extensively used in enamel mineralization efforts [75,76,77,78,79,80][13][14][15][16][17][18]. Notably, these ACP nanoparticles significantly stimulate enamel remineralization, while their instability limits their practical applicability in clinical treatment remarkably [80][18]. ACP has a higher solubility than calcium phosphate crystals and is easily transformed into HAP in solution. Several composites capable of stabilizing ACP have found applications in enamel restoration procedures. Phosphorylated chitosan-stabilized ACP can achieve the remineralization of enamel [76][14]. Casein phosphopeptide-amorphous calcium phosphate (CPP-ACP) can deposit a layer of calcium phosphate mineral on the surface, which has no structure and poor mechanical properties.
Further regulation of the mineralization process is required to obtain an ordered structure. Li et al. demonstrated that the biologically inspired cooperative effect between glutamic acid and nano-apatite particles can result in the regeneration of enamel-like structures under physiological conditions. Importantly, this feasible method of enamel remodeling ensures that the mechanical properties of the repaired enamel are well preserved [81][19]. Wang et al. utilized carboxymethyl chitosan (CMC) and ALN to stabilize ACP into nanoparticles. Sodium hypochlorite degraded the CMC-ALN matrix into HAP@ACP core–shell nanoparticles. Finally, these nanoparticles evolved into rod-like ordered apatite crystals under the guidance of 10 mM glycine [82][20]. However, both oriented and ordered mineral crystals perpendicular to the enamel surface and those parallel to the enamel surface, indicated by red arrows, were found.

2. Dentin Remineralization

2.1. Proteins or Peptides for Dentin Remineralization

According to previous studies, the deposition of HAP within and between collagen fibers is regulated by NCPs, sharing a common characteristic of high serine and aspartic acid content. These amino acids are rich in carboxyl groups and contribute to the overall negative charge of proteins, which enables them to bind to calcium phosphate via interaction with calcium ions, thereby stabilizing amorphous precursors [33,83][21][22]. Consequently, proteins play a crucial role in maintaining the stability of the solution and providing a suitable environment for the subsequent crystallization of the apatite.
The use of natural NCPs is limited by the challenges associated with their extraction, storage, and high cost. However, importantly, the specific sequences present in NCPs play a crucial role in their functionality. Inspired by the structure of NCPs, many biomimetic polypeptide molecules have been designed and synthesized.
The regulatory role of DPP in HAP nucleation and growth is believed to be primarily due to its abundant Asp-Ser-Ser (DSS) repeats. Li et al. used the 8DSS peptide to achieve the remineralization of demineralized dentin [84][23]. 8DSS can interact with dentin collagen, resulting in the formation of mineral precipitates on the surface and within the dentin tubules. The application of 8DSS has a significant positive effect on the elastic modulus and hardness of demineralized dentin and reduces dentin permeability [85][24].
DMP-1 can stabilize calcium and phosphorus ions in solution and generate nucleation precursors. Previous research has shown that the amino acid sequence responsible for collagen adsorption in DMP-1 is linked to certain amino acid sequences responsible for HAP adsorption [86][25]. This association results in the formation of polypeptides that exhibit strong adsorption to type Ⅰ collagen, regulating mineral deposition, stabilizing amorphous precursors formed by calcium and phosphorus ions, and promoting the nucleation and growth of HAP. Additionally, the intermolecular assembly of functional domains within a β-sheet template is essential in the process of mineral nucleation induced by DMP-1 [87][26]. A calcium-responsive self-assembled β-tablet peptide, ID8, has been designed to preprocess collagen [88][27]. The ID8 peptide not only enhances the intermolecular hydrogen bonding but also improves the hydrophilicity of collagen and aids in the retention of calcium within collagen. It has the potential to help regulate collagen mineralization and facilitate the biomimetic mineralization process of early caries [89][28].

2.2. NCP Surrogate

Synthetic analogs of natural NCPs are frequently employed to address the limitations associated with natural NCPs. These analogs are designed to mimic the function of natural NCPs and facilitate mineralization within collagen fibers. The theory of polymer-induced liquid precursors (PILP) is an important approach in the fabrication of mineralized collagen fibers. According to the theory of PILP, the inclusion of these charged polymers in the solution can effectively stabilize the calcium phosphate clusters during the early stages of remineralization, preventing their transformation into HAP crystals [34,91][29][30]. The PILP can infiltrate into the collagen fibers via capillary action and subsequently interact with the binding sites on the collagen fibers, and over time the occurrence of crystallization produces the well-organized mineralized collagen fibers. The use of NCPs analogs commonly includes polyaspartic acid (p-Asp), polyacrylic acid (PAA), CMC, polyglutamic acid(p-Glu), PAMAM, and poly(allylamine) hydrochloride (PAH), etc.
Gower et al. used p-Asp to stabilize ACP and achieve the intrafibrillar mineralization of collagen fibers and proposed the PILP mechanism by which collagen mineralization occurs [92][31]. By using p-Asp as an analog of NCPs, the process of the remineralization of artificial caries was successfully achieved [93][32], resulting in an increase in mineral content within the collagen fiber, improved crystallinity, and the restoration of mechanical properties in the damaged dentin area [94][33]. HAP crystals overgrew on the surface of the mineralized collagen and firmly adhered to the tubule wall, resulting in a compact occlusion of the dentin tubules [44][34].
Another polyelectrolyte, PAA, which is one of the most widely used in the study of collagen mineralization, can mimic the functions of NCPs and is relatively low in cost. Its molecular weight and concentration could affect the mineralization process; as the concentration of PAA increases and the molecular weight of PAA decreases, the crystallization rate of HAP decreases, thus affecting the mineralization degree of collagen fibers. This is mainly because of the variations in the efficiency of PAA/Ca complexation, as well as the influence of PAA molecular weight migration on precursor adsorption efficiency [95,96,97][35][36][37].
These polyelectrolytes could interact strongly with calcium phosphate minerals, stabilizing ACP and inhibiting the nucleation of HAP, thereby inducing intrafibrillar mineralization. It seems unlikely that intrafibrillar mineralized collagen fibrils with a higher degree of mineralization could be obtained in a mineralized system without NCP or its surrogates.

2.3. Based on the Promotion of Collagen Remineralization for the Repair of Dentin

In the process of collagen mineralization, in addition to emphasizing the stabilizing effect of NCPs on ACP precursors, attention is also given to the ability of NCPs to bind calcium and collagen, attract ACP precursors, promote their penetration into the fiber, and initiate nucleation at specific collagen sites. Matrix phosphoproteins irreversibly bind to collagen in hard tissue, providing a template function by which negatively charged phosphate esters bind to positively charged interstitial regions in collagen, forming a negatively charged surface [98,99,100][38][39][40]. The increased local ion oversaturation created on this surface facilitates the nucleation and growth of HAP.
Several phosphorus-containing reagents, such as polyvinylphosphonic acid (PVPA), sodium trimetaphosphate (STMP), and sodium tripolyphosphate (STPP), are used as template analogs to anchor collagen fibers and induce intrafibrillar mineralization. Using PAA and PVPA as dual biomimetic analogues in Portland cement/phosphate-containing solution systems, the remineralization of etched-dentin to a depth of approximately 5 μm has been achieved with interfibrillar and intrafibrillar remineralization [101][41], as well as the remineralization of the resin–dentin interface [102][42]. STMP and STPP can be fixed to collagen by chemical phosphorylation and irreversible binding sites for phosphate groups on the dentin surface [103][43]. When dentin is treated with STMP, HAP forms in the phosphorylated collagen matrix within the fibers, inducing collagen mineralization and achieving artificial caries recrystallization [104][44].

2.4. ACP Nanoparticles for Dentin Remineralization

The mineralization theory based on PILP has been widely recognized and studied. However, its application in the real oral environment is challenging due to the requirement of saturated calcium and phosphorus ion concentration. It is difficult to continuously provide a sufficient concentration of calcium and phosphate for mineralization in the oral cavity. As a precursor to mineralization, ACP is prone to phase transition in solution. Constructing a proper stabilization and transport system for ACP is an excellent strategy for remineralization, allowing for the backfilling of ACP into demineralized dentin and collagen.
The delivery system utilizes a range of materials, such as polycaprolactone, chitosan, PLGA, and mesoporous silica. Several studies have loaded ACP into mesoporous nanoparticles [111,112][45][46]. For example, amine-functionalized enlarged pore silica nanoparticles (AF-eMSN) attached to PAA-ACP successfully achieved mineralization, which is the first attempt to deliver ACP by using enlarged pore silica for mineralization in collagen fibers [113][47]. Using zirconia, a biocompatible ceramic commonly used in dentistry, to synthesize mesoporous nanocapsules loaded with PAH-ACP, the released PAH-ACP still retains its ability to penetrate and mineralize collagen fibers [110][48].
Considering the process of composite resin adhesion and the issues of collagen degradation and microleakage at the demineralized collagen interface, the incorporation of ACP particles into self-etching adhesives or resins is a strategy that has been extensively studied. The use of self-etching adhesives as a carrier of ACP nanoprecursors facilitates continuous biomimetic remineralization [114][49]. Core-shell chlorhexidine/ACP (CHX/ACP) nanoparticles have been synthesized and utilized to enhance dental resin composites, providing them with exceptional mechanical strength, antimicrobial activity, and remineralization capabilities [115][50]. These strategies could further release calcium and phosphate ions to create supersaturation relative to the HAP crystals, and could also infiltrate directly into the fibers, leading to intrafibrillar mineralization, which shows promise for clinical applications.

References

  1. Moradian-Oldak, J.; Simmer, J.P.; Lau, E.C.; Sarte, P.E.; Fincham, A.G. Detection of monodisperse aggregates of a recombinant amelogenin by dynamic light scattering. Biopolymers 2010, 34, 1339–1347.
  2. Engelberth, S.A.; Bacino, M.S.; Sandhu, S.; Li, W.; Bonde, J.; Habelitz, S. Progression of self-assembly of amelogenin protein supramolecular structures in simulated enamel fluid. Biomacromolecules 2018, 19, 3917–3924.
  3. Du, C.; Falini, G.; Fermani, S.; Abbott, C.; Moradian-Oldak, J. Supramolecular Assembly of Amelogenin Nanospheres into Birefringent Microribbons. Science 2005, 307, 1450–1454.
  4. Fincham, A.G.; Moradian-Oldak, J.; Diekwisch, T.G.H.; Lyaruu, D.M.; Wright, J.T.; Bringas, P.; Slavkin, H.C. Evidence for amelogenin “Nanospheres” as functional components of secretory-stage enamel matrix. J. Struct. Biol. 1995, 115, 50–59.
  5. Ren, Q.; Li, Z.; Ding, L.; Wang, X.; Niu, Y.; Qin, X.; Zhou, X.; Zhang, L. Anti-biofilm and remineralization effects of chitosan hydrogel containing amelogenin-derived peptide on initial caries lesions. Regen. Biomater. 2018, 5, 69–76.
  6. Ding, L.J.; Han, S.L.; Wang, K.; Zheng, S.N.; Zheng, W.Y.; Peng, X.; Niu, Y.M.; Li, W.; Zhang, L.L. Remineralization of enamel caries by an amelogenin-derived peptide and fluoride in vitro. Regen. Biomater. 2020, 7, 283–292.
  7. Yang, S.; He, H.; Wang, L.; Jia, X.; Feng, H. Oriented crystallization of hydroxyapatite by the biomimetic amelogenin nanospheres from self-assemblies of amphiphilic dendrons. Chem. Commun. 2011, 47, 10100–10102.
  8. Yang, J.; Cao, S.; Li, J.; Xin, J.; Chen, X.; Wu, W.; Xu, F.; Li, J. Staged self-assembly of PAMAM dendrimers into macroscopic aggregates with a microribbon structure similar to that of amelogenin. Soft Matter 2013, 9, 7553–7559.
  9. Mahamid, J.; Sharir, A.; Addadi, L.; Weiner, S. Amorphous calcium phosphate is a major component of the forming fin bones of zebrafish: Indications for an amorphous precursor phase. Proc. Natl. Acad. Sci. USA 2008, 105, 12748–12753.
  10. Steve, W.; Julia, M.; Yael, P.; Yurong, M.A.; Lia, A. Overview of the amorphous precursor phase strategy in biomineralization. Front. Mater. Sci. China 2009, 3, 104–108.
  11. Lowenstam, H.A.; Weiner, S. Transformation of amorphous calcium phosphate to crystalline dahillite in the radular teeth of chitons. Science 1985, 227, 51–53.
  12. Beniash, E.; Metzler, R.A.; Lam, R.S.K.; Gilbert, P. Transient amorphous calcium phosphate in forming enamel. J. Struct. Biol. 2009, 166, 133–143.
  13. Zhao, J.; Liu, Y.; Zhang, S.H. Amorphous calcium phosphate and its application in dentistry. Chem. Cent. J. 2011, 5, 7.
  14. Zhang, X.; Li, Y.; Sun, X.; Kishen, A.; Deng, X.; Yang, X.; Wang, H.; Cong, C.; Wang, Y.; Wu, M. Biomimetic remineralization of demineralized enamel with nano-complexes of phosphorylated chitosan and amorphous calcium phosphate. J. Mater. Sci. Mater. Med. 2014, 25, 2619–2628.
  15. Fletcher, J.; Walsh, D.; Fowler, C.E.; Mann, S. Electrospun mats of PVP/ACP nanofibres for remineralization of enamel tooth surfaces. CrystEngComm 2011, 13, 3692–3697.
  16. Iafisco, M.; Degli Esposti, L.; Ramirez-Rodriguez, G.B.; Carella, F.; Gomez-Morales, J.; Ionescu, A.C.; Brambilla, E.; Tampieri, A.; Delgado-Lopez, J.M. Fluoride-doped amorphous calcium phosphate nanoparticles as a promising biomimetic material for dental remineralization. Sci. Rep. 2018, 8, 17016.
  17. Xiao, Z.H.; Que, K.H.; Wang, H.R.; An, R.; Chen, Z.; Qiu, Z.J.; Lin, M.L.; Song, J.H.; Yang, J.; Lu, D.Y.; et al. Rapid biomimetic remineralization of the demineralized enamel surface using nano-particles of amorphous calcium phosphate guided by chimaeric peptides. Dent. Mater. 2017, 33, 1217–1228.
  18. Weir, M.D.; Chow, L.C.; Xu, H.H.K. Remineralization of Demineralized Enamel via Calcium Phosphate Nanocomposite. J. Dent. Res. 2012, 91, 979–984.
  19. Li, L.; Mao, C.Y.; Wang, J.M.; Xu, X.R.; Pan, H.H.; Deng, Y.; Gu, X.H.; Tang, R.K. Bio-inspired enamel repair via Glu-directed assembly of apatite nanoparticles: An approach to biomaterials with optimal characteristics. Adv. Mater. 2011, 23, 4695–4701.
  20. Wang, H.R.; Xiao, Z.H.; Yang, J.; Lu, D.Y.; Kishen, A.; Li, Y.Q.; Chen, Z.; Que, K.H.; Zhang, Q.; Deng, X.L.; et al. Oriented and ordered biomimetic remineralization of the surface of demineralized dental enamel using HAP@ACP nanoparticles guided by glycine. Sci. Rep. 2017, 7, 40701.
  21. Deshpande, A.S.; Fang, P.-A.; Zhang, X.; Jayaraman, T.; Sfeir, C.; Beniash, E. Primary Structure and phosphorylation of dentin matrix protein 1 (DMP1) and dentin phosphophoryn (DPP) uniquely determine their role in biomineralization. Biomacromolecules 2011, 12, 2933–2945.
  22. Gericke, A.; Qin, C.; Sun, Y.; Redfern, R.; Redfern, D.; Fujimoto, Y.; Taleb, H.; Butler, W.T.; Boskey, A.L. Different forms of DMP1 play distinct roles in mineralization. J. Dent. Res. 2010, 89, 355–359.
  23. Liang, K.; Xiao, S.; Shi, W.; Li, J.; Yang, X.; Gao, Y.; Gou, Y.; Hao, L.; He, L.; Cheng, L.; et al. 8DSS-promoted remineralization of demineralized dentin in vitro. J. Mater. Chem. B 2015, 3, 6763–6772.
  24. Liang, K.; Xiao, S.; Liu, H.; Shi, W.; Li, J.; Gao, Y.; He, L.; Zhou, X.; Li, J. 8DSS peptide induced effective dentinal tubule occlusion in vitro. Dent. Mater. 2018, 34, 629–640.
  25. Padovano, J.D.; Ravindran, S.; Snee, P.T.; Ramachandran, A.; Bedran-Russo, A.K.; George, A. DMP1-derived peptides promote remineralization of human dentin. J. Dent. Res. 2015, 94, 608–614.
  26. He, G.; Dahl, T.; Veis, A.; George, A. Nucleation of apatite crystals in vitro by self-assembled dentin matrix protein 1. Nat. Mater. 2003, 2, 552–558.
  27. Li, Z.; Ren, Q.; Han, S.; Ding, L.; Qin, X.; Hui, D.; Het, T.; Tian, T.; Lu, Z.; Zhang, L. Promoting effect of a calcium-responsive self-assembly β-sheet peptide on collagen intrafibrillar mineralization. Regen. Biomater. 2022, 9, rbac059.
  28. Li, Z.C.; Qin, X.; Ren, Q.; Hui, D.; Tian, T.; He, T.; Li, W.; Zhang, L.L. Rational design of β-sheet peptides with self-assembly into nanofibres on remineralisation of initial caries lesions. Chin. J. Dent. Res. 2020, 23, 131–141.
  29. Nudelman, F.; Pieterse, K.; George, A.; Bomans, P.H.H.; Friedrich, H.; Brylka, L.J.; Hilbers, P.A.J.; de With, G.; Sommerdijk, N.A.J.M. The role of collagen in bone apatite formation in the presence of hydroxyapatite nucleation inhibitors. Nat. Mater. 2010, 9, 1004–1009.
  30. Olszta, M.J.; Cheng, X.; Jee, S.S.; Kumar, R.; Kim, Y.-Y.; Kaufman, M.J.; Douglas, E.P.; Gower, L.B. Bone structure and formation: A new perspective. Mater. Sci. Eng. R. Rep. 2007, 58, 77–116.
  31. Gower, L.B.; Odom, D.J. Deposition of calcium carbonate films by a polymer-induced liquid-precursor (PILP) process. J. Cryst. Growth 2000, 210, 719–734.
  32. Burwell, A.K.; Thula-Mata, T.; Gower, L.B.; Habeliz, S.; Kurylo, M.; Ho, S.P.; Chien, Y.-C.; Cheng, J.; Cheng, N.F.; Gansky, S.A.; et al. Functional remineralization of dentin lesions using polymer-induced liquid-precursor process. PLoS ONE 2012, 7, e38852.
  33. Bacino, M.; Girn, V.; Nurrohman, H.; Saeki, K.; Marshall, S.J.; Gower, L.; Saeed, E.; Stewart, R.; Le, T.; Marshall, G.W.; et al. Integrating the PILP-mineralization process into a restorative dental treatment. Dent. Mater. 2019, 35, 53–63.
  34. Chen, Z.; Duan, Y.; Shan, S.; Sun, K.; Wang, G.; Shao, C.; Tang, Z.; Xu, Z.; Zhou, Y.; Chen, Z.; et al. Deep and compact dentinal tubule occlusion via biomimetic mineralization and mineral overgrowth. Nanoscale 2022, 14, 642–652.
  35. Qi, Y.; Ye, Z.; Fok, A.; Holmes, B.N.; Espanol, M.; Ginebra, M.-P.; Aparicio, C. Effects of molecular weight and concentration of poly(Acrylic Acid) on biomimetic mineralization of collagen. ACS Biomater. Sci. Eng. 2018, 4, 2758–2766.
  36. Shen, L.; Bu, H.; Zhang, Y.; Tang, P.; Li, G. Molecular weight and concentration of poly (acrylic acid) dual-responsive homogeneous and intrafibrillar collagen mineralization using an in situ co-organization strategy. Polym. Compos. 2021, 42, 4448–4460.
  37. Chen, L.; Zeng, Z.; Li, W. Poly(acrylic acid)-assisted intrafibrillar mineralization of type I collagen: A review. Macromol. Rapid Commun. 2023, 44, e2200827.
  38. Butler, W.T. Dentin matrix proteins. Eur. J. Oral Sci. 1998, 106, 204–210.
  39. Gulseren, G.; Tansik, G.; Garifullin, R.; Tekinay, A.B.; Guler, M.O. Dentin phosphoprotein mimetic peptide nanofibers promote biomineralization. Macromol. Biosci. 2019, 19, e1800080.
  40. Prasad, M.; Butler, W.T.; Qin, C. Dentin sialophosphoprotein in biomineralization. Connect. Tissue Res. 2010, 51, 404–417.
  41. Tay, F.R.; Pashley, D.H. Guided tissue remineralisation of partially demineralised human dentine. Biomaterials 2008, 29, 1127–1137.
  42. Mai, S.; Kim, Y.K.; Toledano, M.; Breschi, L.; Ling, J.Q.; Pashley, D.H.; Tay, F.R. Phosphoric acid esters cannot replace polyvinylphosphonic acid as phosphoprotein analogs in biomimetic remineralization of resin-bonded dentin. Dent. Mater. 2009, 25, 1230–1239.
  43. Gu, L.-S.; Kim, J.; Kim, Y.K.; Liu, Y.; Dickens, S.H.; Pashley, D.H.; Ling, J.-Q.; Tay, F.R. A chemical phosphorylation-inspired design for Type I collagen biomimetic remineralization. Dent. Mater. 2010, 26, 1077–1089.
  44. Liu, Y.; Li, N.; Qi, Y.; Niu, L.-N.; Elshafiy, S.; Mao, J.; Breschi, L.; Pashley, D.H.; Tay, F.R. The use of sodium trimetaphosphate as a biomimetic analog of matrix phosphoproteins for remineralization of artificial caries-like dentin. Dent. Mater. 2011, 27, 465–477.
  45. Cuylear, D.L.; Elghazali, N.A.; Kapila, S.D.; Desai, T.A. Calcium phosphate delivery systems for regeneration and biomineralization of mineralized tissues of the craniofacial complex. Mol. Pharm. 2023, 20, 810–828.
  46. Wei, J.; Shi, J.; Wu, Q.; Yang, L.; Cao, S. Hollow hydroxyapatite/polyelectrolyte hybrid microparticles with controllable size, wall thickness and drug delivery properties. J. Mater. Chem. B 2015, 3, 8162–8169.
  47. Luo, X.-J.; Yang, H.-Y.; Niu, L.-N.; Mao, J.; Huang, C.; Pashley, D.H.; Tay, F.R. Translation of a solution-based biomineralization concept into a carrier-based delivery system via the use of expanded-pore mesoporous silica. Acta Biomater. 2016, 31, 378–387.
  48. Huang, X.-Q.; Yang, H.-Y.; Luo, T.; Huang, C.; Tay, F.R.; Niu, L.-N. Hollow mesoporous zirconia delivery system for biomineralization precursors. Acta Biomater. 2018, 67, 366–377.
  49. Abuna, G.; Feitosa, V.P.; Correr, A.B.; Cama, G.; Giannini, M.; Sinhoreti, M.A.; Pashley, D.H.; Sauro, S. Bonding performance of experimental bioactive/biomimetic self-etch adhesives doped with calcium-phosphate fillers and biomimetic analogs of phosphoproteins. J. Dent. 2016, 52, 79–86.
  50. Yang, Y.; Xu, Z.; Guo, Y.; Zhang, H.; Qiu, Y.; Li, J.; Ma, D.; Li, Z.; Zhen, P.; Liu, B.; et al. Novel core-shell CHX/ACP nanoparticles effectively improve the mechanical, antibacterial and remineralized properties of the dental resin composite. Dent. Mater. 2021, 37, 636–647.
More
© Text is available under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/)
Video Production Service
Feedback