Multifunctional Primer for Dentin Bonding via Biomimetic Mineralization

Abstract

Enhancing the durability of dentin bonding remains a significant challenge in dental restoration. This study introduces an innovative approach using aldehyde-grafted polyaspartate (PACA) to achieve spatiotemporal regulation of biomimetic mineralization through collagen cross-linking. The collagen cross-linking capability of PACA was confirmed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis. Its ability to induce intrafibrillar mineralization of collagen fibrils was investigated using a rat tail collagen model through dynamic light scattering, zeta potential measurements, and transmission electron microscopy. In addition, the remineralization efficacy of PACA on demineralized dentin collagen was evaluated using scanning electron microscopy, energy dispersive X-ray spectroscopy, and atomic force microscopy. These analyses revealed that PACA facilitates intrafibrillar mineralization by creating an amorphous calcium phosphate–rich microenvironment in the cross-linked region. Subsequently, the mineralization encapsulates the covalently cross-linked polymer and collagen fibrils within a mineralized matrix, forming an organized crystalline structure. Furthermore, PACA was used as a single-component primer in a dentin bonding model, and its impact on bonding durability was assessed through micro-tensile bond strength testing, nanoleakage analysis, and in situ zymography. These assessments demonstrate that PACA could simultaneously achieve collagen cross-linking, matrix metalloproteinase inhibition, and enhanced adhesive penetration while facilitating temporally regulated mineralization. Due to this multifunctionality, the PACA primer significantly improves micro-tensile bond strength and exhibits favorable durability after the aging experiment. This innovative approach provides a promising solution to the durability limitations of conventional adhesive systems.

Keywords

collagen biomineralization hydroxyapatites dental adhesives cross-linking reagents matrix metalloproteinase inhibitors

Introduction

Dental caries, the most prevalent noncommunicable disease worldwide, often presents with lesions that may require restorative treatment with composite resins to restore tooth morphology and function. Dentin adhesive systems play a crucial role in the restoration process. The 3-step etch-and-rinse technique remains the gold standard for dentin bonding (Van Meerbeek et al. 2020). It relies on adhesive monomers that infiltrate the demineralized collagen to form a micromechanical interlocking structure, known as the hybrid layer (Tjäderhane et al. 2013). The hybrid layer is expected to exhibit favorable durability by maintaining long-term mechanical strength and a stable marginal seal. However, incomplete infiltration of adhesive monomers into water-saturated collagen fibrils results in exposed collagen at the base of the hybrid layer, which forms a vulnerable zone (Betancourt et al. 2019). This exposed collagen, which lacks mineral or resin coverage, is highly prone to enzymatic degradation (Breschi et al. 2018), while a water-filled gap zone create a favorable microenvironment for resin hydrolysis, progressively compromising bond integrity and ultimately leading to bonding failure (Kim, Mai, et al. 2010; Liu, Li, et al. 2011).

Hybrid layer remineralization improves dentin bonding durability (Sauro et al. 2015) but requires months, leaving collagen susceptible to matrix metalloproteinases (MMPs) and cysteine degradation (Tjäderhane et al. 2013). These endogenous enzymes can be sustainably inhibited by collagen cross-linking agents that simultaneously reinforce the collagen fibril network (Matos et al. 2017). Aldehyde-based compounds, particularly glutaraldehyde, represent typical collagen cross-linking agents, are particularly effective due to their strong cross-linking capabilities, rapidly forming covalent bonds with collagen fibrils through Schiff base (-C=N-) reactions (Yu et al. 2022), and have been shown to not only strengthen dentin collagen but also serve as a template for biomimetic remineralization (Chen et al. 2016). Despite their functional advantages, the biosafety of aldehydes remains a concern.

The remineralization of demineralized collagen not only protects it from enzymatic hydrolysis but also reduces the risk of resin hydrolysis by replacing water with mineral crystals (Niu et al. 2014). However, with classical nucleation theory, remineralization of dentin collagen resulted in only extrafibrillar mineral deposition (Kim, Arola, et al. 2010). Olszta et al. (2007) pioneered the polymer-induced liquid-precursor (PILP) process, demonstrating how noncollagenous protein (NCP) analogues stabilize amorphous calcium phosphate (ACP), facilitating its infiltration into collagen fibrils to achieve intrafibrillar mineralization. Subsequent research has enhanced this biomimetic process by developing various synthetic NCP analogues with dual functionalities: (1) calcium phosphate nucleation inhibitors that stabilize mineral precursors, exemplified by polyacrylic acid (Wu et al. 2017) and polyaspartate (PASP) and (2) template agents that guide the controlled deposition of minerals onto collagen fibrils, such as polyphosphate-containing biomimetic analog (Gu et al. 2011; Liu, Li, et al. 2011). Despite these advances, a significant limitation persists: all current approaches necessitate the incorporation of nucleation inhibitors directly into calcium phosphate precursor solutions (Ca/P) to generate the requisite amorphous liquid-phase intermediates, which limits its practical usage.

To address these limitations, a polymer of aldehyde-grafted polyaspartate (PACA) was designed as a multifunctional primer. This study aimed to enhance the durability of dentin bonding through combined collagen cross-linking and biomimetic mineralization strategies. The grafted aldehyde groups are expected to covalently cross-link with collagen fibrils as a short-term strategy to strengthen the hybrid layer (Breschi et al. 2018). Meanwhile, the PACA polymer preserves the capability of PASP to induce intrafibrillar mineralization for achieving a long-term strategy for hybrid layer reinforcement. Critically, the covalent attachment eliminates the requirement for free PASP in the Ca/P solution during the PILP process. Based on the experimental findings, this multifunctional design facilitates spatiotemporal modulation of dentin biomimetic remineralization and provides insights into how mineralization patterns may influence bonding longevity.

Materials and Methods

Synthesis and Characterization of PACA

As shown in Figure 1A, polysuccinimide (PSI) was dissolved in dimethylformamide and reacted with 3-amino-1,2-propanediol (2 mmol/mL) at molar ratios of 10%, 30%, and 50% at 40 °C for 10 h, yielding 3-amino-1,2-propanediol-grafted polysuccinimide (APD-PSI) precipitates, which were subsequently hydrolyzed with NaOH to produce APD-PASP. Subsequent reaction with sodium periodate (0.33 M) at 0 °C for 30 min, followed by dialysis and lyophilization, yielded aldehyde-grafted polyaspartic acid (PACA-1, PACA-2, PACA-3) (Gu et al. 2013; Lu et al. 2014). Fourier transform infrared (FTIR) spectroscopy, ¹H nuclear magnetic resonance (NMR), and gel permeation chromatography (GPC) were used to characterize PACA. Details are provided in the Appendix.

Mineralization within Single-Layer Collagen Fibrils

Lyophilized rat tail collagen powder (Sigma-Aldrich) was dissolved in acetic acid, diluted with phosphate-buffered saline buffer, pH adjusted to 7 with NaOH, and incubated at 37 °C for 3 d to promote collagen fibril self-assembly. Collagen fibrils were cross-linked with PACA (240 µg/mL) for 1 h and subsequently purified by ultrafiltration, with PASP as a control. sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) was used to evaluate the impact of chemical cross-linking on collagen. The zeta potential of PACA and PACA cross-linked rat tail collagen (1 mg/mL) assessed the effects on electronegativity. Dynamic light scattering (DLS) examined how PACA and PASP influenced particle size distribution in calcium phosphate solutions.

Transmission Electron Microscopy and Selected Area Electron Diffraction

A single-layer collagen fibril model was constructed by depositing a 10 µL of collagen fibril self-assembly solution (0.1 mg/mL) onto a nickel mesh (Fig. 2A). The fibrils were subsequently cross-linked for 1 h and subjected to mineralization in a Ca/P solution (2.7 mM CaCl2, 1.35 mM K2HPO4, and 10 mM HEPES) for 1, 3, and 5 d. The PILP process served as a positive group through adding PASP to the Ca/P solution. This preparation was conducted for analysis via transmission electron microscopy (TEM) and selected area electron diffraction (SAED) to evaluate the morphology and crystallographic properties of the mineral deposits.

Molecular Dynamics Simulations

Molecular dynamics (MD) simulations (Fig. 3) were conducted for 50 ns using GROMACS 2021.4 software package to investigate the conformational dynamics of PACA–cross-linked collagen (PDB ID: 1QSU) under position restraints. The simulation system was solvated in an explicit water box containing 60 calcium ions (Ca²+) and 40 phosphate ions (PO4³–).

Mineralization of Dentin Collagen Fibrils

Hydroxyproline release

Demineralized dentin collagen (150 mg) was mixed with PACA (1 mL) for 1 min and freeze-dried to yield cross-linked collagen, then 100 mg cross-linked collagen was incubated in a collagenase solution (1.5 mL) at 37 °C for 24 h, after which the hydroxyproline (HYP) content in the supernatant was quantified. Details of the demineralized dentin collagen powder and collagenase solution preparation are provided in the Appendix.

Remineralization of demineralized dentin disk surfaces

Sixty 1-mm-thick dentin disks were prepared by sectioning noncarious human molars perpendicular to the longitudinal axis. After etching with 37% phosphoric acid gel for 15 s, PACA was applied to the surfaces for 1 min (Fig. 4A). Dentin disks treated with PASP alone served as a negative control, while PASP added to the Ca/P solution served as a positive control. Surface mineralization of the samples was examined using scanning electron microscopy (SEM), and energy-dispersive spectroscopy (EDS) was used to analyze the calcium (Ca) and phosphorus (P) content on the surface (n = 3). The mechanical properties of biomimetic mineralized collagen were analyzed using atomic force microscopy (AFM) under the PeakForce QNM mode (2 data points × 3 specimens; n = 6).

Impact of PACA Primer on the Durability of Dentin Bonding

Micro-tensile bond strength

The preparation of the dentin bonding model and micro-tensile bond strength (µTBS) samples are detailed in the Appendix. An etch-and-rinse technique evaluated 4 experimental primers (15 mg/mL PASP, PACA-1, PACA-2, and PACA-3) formulated in 20 mM Hepes buffer (pH 7), using Single Bond Universal as the commercial adhesive reference, with PASP designated as the negative control and deionized water as the blank control. Samples were divided into the immediate group (24 h in deionized water at 37 °C), mineralization group (7 d in Ca/P solution at 37 °C under simulated medullary cavity pressure), and thermocycled group (10,000 cycles between 5 °C and 55 °C water baths, 30 s each). Fracture samples were platinum coated for 1 min and examined by SEM and EDS, with data expressed as mean ± standard deviation (n = 3).

Confocal laser scanning microscopy

PACA primers were mixed with rhodamine B (0.1 wt%, 535/605 nm), while Scotchbond Universal adhesive contained sodium fluorescein (0.1 wt%, Ex/Em = 490/525 nm). After 24 h at 37 °C, 1 mm resin–dentin sections (n = 3) were examined at a wavelength of 488/568 nm.

In situ zymography

In situ zymography was performed with the EnzChek Gelatinase/Collagenase Assay Kit. Bonding samples were sliced to 1 mm, incubated with 80 µL gelatin stock solution at 37 °C for 24 h, and then visualized using confocal laser scanning microscopy at ex/em = 488/533 nm.

Nanoleakage evaluation

For nanoleakage, samples were immersed in 50% silver ammonia nitrate for 24 h, exposed to fluorescent light for 8 h in a photo-developing solution, and analyzed with SEM and EDS.

Statistical Analysis

Statistical analyses were conducted using Prism software (version 10; GraphPad Software). The Shapiro–Wilk test checked data normality, and the Levene test assessed variance equality. Two-way analyses of variance (ANOVAs) analyzed SDS-PAGE, EDS, AFM, and µTBS results, while 1-way ANOVA was used for Zeta potential, CCK-8, and HYP release data. Tukey’s multiple comparison test was applied for pairwise comparisons, with the significance level set at α = 0.05.

Results

Synthesis and Characterization of PACA

FTIR spectroscopy was used to monitor structural transformations during the synthesis. As shown in Figure 1B, the peak at 1,713.6 cm–¹ is indicative of succinimide rings in PSI (Adelnia et al. 2021). Grafting resulted in ring-opening aminolysis, evidenced by emerging amide I (1,657 cm–¹) and II (1,540 cm–¹) peaks (Fig. 1B). Hydrolysis eliminated the 1,714 cm–¹ peak, confirming full conversion to amide structures (Fig. 1C). Oxidation introduced aldehyde groups, as seen by a new peak at 1,715 cm–¹ (Fig. 1D).

¹H NMR (Fig. 1E) analysis revealed that aldehyde groups in PACA series compounds existed in dynamic equilibrium with 1,1-diol forms in aqueous solution, resulting in weak aldehyde proton signals at δ = 9.42 ppm and characteristic 1,1-diol peaks at δ = 4.99 ppm (Gu et al. 2013). Based on ¹H NMR integration, aldehyde grafting degrees for PACA-2 and PACA-3 were calculated as 14% and 33%, respectively, while PACA-1’s ratio was too low to quantify. GPC analysis (Appendix Table S1) showed increasing molecular weight (Mw) with increasing feed ratio, with polymerization degrees of 156, 169, and 183 for PACA-1, PACA-2, and PACA-3 respectively.

Mineralization within Single-Layer Collagen Fibrils

SDS-PAGE (Fig. 2B) and ImageJ gray-scale analysis (Fig. 2C) revealed that PACA-2 and PACA-3 groups with higher aldehyde content not only increased peptide chains (P < 0.05) but also generated peptide chains with molecular weights exceeding those of γ and β chains (Visser et al. 2023), confirming the formation of covalent cross-linking.

Zeta potential analyses showed that increasing aldehyde content slightly reduced polymer electronegativity (Fig. 2D), while PACA-2 and PACA-3 cross-linked collagen exhibited increased electronegativity compared with PASP-treated collagen (Fig. 2E).

DLS analysis showed freshly mineralized PASP solution contained uniform ~60 nm Ca/P particles, while PACA-2 and PACA-3 produced 3 distinct size distributions: 10 to 20 nm (prenucleation clusters), 60 nm (ACPs), and 220 nm (polymer–ACP aggregates) (Fig. 2F). After 7 d, the PACA groups demonstrated inferior long-term ACP stability compared with PASP (Fig. 2G).

TEM analysis of single-layer rat tail collagen showed PASP-treated samples in Ca/P solution lacked adequate intrafibrillar mineralization (Fig. 2I, N, S). The positive control using the PILP process achieved significant mineralization within 5 d (Fig. 2Q), while PACA-treated groups displayed distinct mineralization by day 3. SAED patterns confirmed crystalline hydroxyapatite formation, with initial diffuse patterns indicating amorphous minerals (Fig. 2J, K, L, O, P) (Gu et al. 2011). By day 3, PACA-3 group exhibited a distinct (002) plane (Fig. 2Q), showing HAp c-axis alignment parallel to the collagen fibrils’ longitudinal axis—similar to natural dentin. The (211), (112), and (300) planes formed continuous diffuse rings (d = 2.814, 2.778, 2.720 Å), while (004) diffraction arches confirmed c-axis needle-like minerals parallel to fibrils (Amornkitbamrung et al. 2022).

MD simulation (Fig. 3A) showed calcium ions and phosphate initially distributed uniformly around PACA–cross-linked collagen. After 10 ns, CaP aggregates formed larger particles away from PACA, while some Ca²+ remained chelated around the polymer. By 50 ns, most CaP aggregated into large particles away from the polymer, while free calcium ions remained around it. Radial distribution function (RDF) analysis (Fig. 3B) Ca²+ aggregated on the protein surface, while PO4³^- were more dispersed. Interaction energy analysis indicated Ca²+ had a van der Waals energy of 46.99 kJ/mol (Fig. 3F) and a strong electrostatic attraction of −2,701.43 kJ/mol (Fig. 3E). PO4³^- had a van der Waals energy of −32.07 kJ/mol (Fig. 3E) and an electrostatic repulsion of 1,261.13 kJ/mol (Fig. 3D).

Mineralization of Dentin Collagen Fibrils

As depicted in Figure 4B, both the 15 mg/mL and 30 mg/mL concentrations of PACA-2 and PACA-3 exhibited a significant decrease in HYP release. Therefore, 15 mg/mL was chosen as the optimal final concentration.

SEM (Fig. 4C) and EDS (Fig. 4D) analyses revealed PACA-treated samples mineralized faster than PASP controls did, with positive controls showing only 36% mineralization after 7 d. Higher cross-linking in the PACA-2 and PACA-3 groups achieved greater mineralization degrees (59.9% and 68.7%). After 7 d, these groups displayed orderly CaP crystal deposition aligned with collagen fiber orientation—a feature absent in the positive group, which showed spherical extrafibrillar crystals (Chen et al. 2020). The crystal c-axis of interfibrillar minerals aligned parallel to collagen fiber orientation, demonstrating ordered mineralization that likely resulted from epitaxial growth using intrafibrillar mineralized collagen as nucleation sites (Wu et al. 2021).

The AFM results in Figure 4E reveal the collagen matrix transitioning from pink to purple, indicating improved mechanical properties. The positive group showed an orderly DMT modulus increase between days 4 and 7, while PASP demonstrated more extensive calcium phosphate deposition. The DMT modulus showed no statistically significant difference between PACA and positive control groups (P > 0.05); however, PACA exhibited significantly different modulus values compared with the PASP groups (P < 0.05). The DMT modulus of the PACA-3 group increased significantly over time, reaching 11.7 GPa at day 7 (P < 0.05) (Fig. 4F).

Impact of PACA Primer on the Durability of Dentin Bonding

The µTBS testing revealed that PACA primer exhibited significantly higher immediate bond strength values compared with the control group (P < 0.05, 2-way ANOVA, Tukey’s post hoc test) (Fig. 5B). The mineralization process alone contributed minimally to the enhancement of µTBS (P > 0.05). Following accelerated aging via thermocycling, specimens treated with PACA-3 primer maintained statistically stable µTBS (P > 0.05). In contrast, control specimens exhibited significant µTBS degradation after thermocycling aging (P < 0.05).

Failure analysis (Fig. 5C) revealed that the PACA groups had a higher incidence of cohesive composite failure postmineralization. Under thermal cycling, PACA-3 showed increased cohesive failure within the composite due to superior mineralization efficiency. EDS scanning (Fig. 5D) confirmed that the degree of mineralization increased with cross-linking degree.

Figure 5E shows that the PACA primer penetrated deeper than PASP did and enhanced subsequent adhesive penetration. In situ zymography (Fig. 5F) demonstrated a sequential reduction in MMP activity at the bonding interface across the PACA-1, PACA-2, and PACA-3 groups, suggesting a correlation between enzyme inhibition and covalent cross-linking. After thermocycling, only PACA-2 and PACA-3 maintained decreased fluorescence intensity. EDS scanning (Fig. 5G) showed that PACA-3 had significantly lower silver nanoleakage than other groups did (P < 0.05).

Discussion

Dentin is a complex mineralized tissue composed of a collagen matrix with hierarchically arranged calcium phosphate crystals distributed within both extrafibrillar and intrafibrillar compartments (Sharma et al. 2021). The classical nucleation pathway and nonclassical crystallization pathway constitute the 2 primary theories for dentin biomineralization (Qin et al. 2022). The classical pathway follows a top-down approach, wherein mineral deposition initiates from a crystal nucleus. However, this approach has achieved limited success in reproducing the hierarchical apatite deposition within the collagen matrix. In contrast, the nonclassical crystallization pathway proceeds via a bottom-up process, facilitating ordered intrafibrillar mineral deposition, which helps explain the formation of the hierarchical structures observed in natural dentin (Niu et al. 2014). Building on the nonclassical pathway, biomimetic mineralization strategies are increasingly being used to enhance the durability of dentin bonding. The use of high-concentration amorphous calcium fluoride solutions (Gao et al. 2024) is considered a promising strategy. Moreover, collagen stabilization (Tao et al. 2022; Hu et al. 2024) and remineralization promoter retention (Fan et al. 2024; Zhu et al. 2025) enabled these promoters to function effectively in dentin.

PACA, which consists of a biodegradable PASP backbone (Adelnia et al. 2021), exhibits remarkable biocompatibility (Appendix Fig. S1). The strategic covalent integration of aldehyde groups into the polymer backbone prevents complete release, even under partial hydrolysis conditions, substantially reducing potential cytotoxicity concerns (Yu et al. 2022).

PACA promotes biomimetic mineralization through 2 key mechanisms. First, its aldehyde moieties form stable covalent cross-links with lysine and hydroxylysine residues within the collagen triple helix (Pereira et al. 2014), as confirmed by distinctive band shifts in SDS-PAGE analysis (Fig. 2B). The HYP release assessment demonstrated a concentration-dependent effect on cross-linking (Fig. 4B; Liu, Tjäderhane, et al. 2011; Matos et al. 2017), with the degree of cross-linking reaching a plateau at 15 mg/mL for both PACA-2 and PACA-3. Second, PACA maintains its electronegativity from PASP (Olszta et al. 2007), which promotes the formation of ACP nanoparticles (Fig. 2D–G). This cross-linking generates heightened ACP concentrations external to collagen fibrils (Fig. 3), establishing osmotic gradients that facilitate precursor infiltration into collagen gap zones (Nudelman et al. 2010; Jiao et al. 2016; Niu et al. 2017). In summary, PACA forms a localized microenvironment around collagen fibrils, creating favorable conditions that significantly accelerate biomimetic mineralization.

TEM and SAED observations (Fig. 2) confirmed intrafibrillar mineralization within PACA-treated collagen fibrils. Notably, the PACA-3 group demonstrated highly ordered intrafibrillar mineralization as early as day 3 (Fig. 2Q). SEM and EDS images (Fig. 4) at day 7 revealed ordered interfibrillar and extrafibrillar mineralization (Wu et al. 2021) in the PACA-3 group, illuminating a sophisticated sequential mineralization mechanism. Initially, intrafibrillar mineralization develops progressively within the ACP-rich microenvironment surrounding the collagen fibrils, which is facilitated by PACA. As mineralization advances, it encapsulates both the covalently cross-linked polymer and collagen fibrils within a mineralized matrix, while PACA’s influence gradually diminishes. This mineralized collagen establishes an organized crystalline nucleus, which initiates a top-down mineralization mechanism that promotes hierarchical mineral accumulation.

Based on established parameters (Liu et al. 2013), AFM analysis demonstrated distinct mineralization patterns among the experimental groups. While the PILP-positive control achieved intrafibrillar mineralization and the PASP group predominantly exhibited extrafibrillar mineralization, PACA-treated specimens displayed DMT modulus values statistically comparable with those of the PILP control. These quantitative data confirm that PACA treatment effectively induces intrafibrillar mineralization and improves the mechanical properties of demineralized dentin collagen matrices (Kinney et al. 2003).

PACA primer significantly enhances dentin bonding through its multifunctional properties, with aldehyde groups cross-linking collagen to preserve dentinal tubule morphology and promote adhesive penetration (Fig. 5E), thereby improving immediate µTBS (Fig. 5B). While PACA-mediated biomimetic mineralization does not directly affect immediate bond strength, it plays a crucial role in long-term durability, with PACA-3 demonstrating superior performance under thermocycling conditions due to its advanced biomimetic mineralization efficiency (Figs. 2Q, 4C) and excellent mechanical properties (Fig. 4E). This single-component primer system provides both short-term MMP inhibition through covalent cross-linking and long-term MMP inhibition via biomimetic mineralization (Figs. 4B, 5F) (Gu et al. 2018), effectively reducing nanoleakage (Fig. 5F) and maintaining bond integrity over time. PACA-3 cleverly uses these complementary mechanisms to achieve hierarchical biomimetic remineralization in improving dentin bonding durability.

Conclusion

As a single-component primer, PACA-3 especially integrates multiple functions, including collagen cross-linking, MMP inhibition, enhanced adhesive penetration, and facilitated temporally regulated mineralization. These properties collectively establish a promising strategy for enhancing the long-term durability of resin–dentin bonds in restorative dentistry.

Author Contributions

S.H. Yang, contributed to conception and design, data acquisition, analysis, and interpretation, drafted and critically revised the manuscript; Z.L. Tian, contributed to data acquisition and analysis, drafted and critically revised the manuscript; H.M. Wang, contributed to data acquisition and analysis, critically revised the manuscript; D. Sun, contributed to data analysis, drafted and critically revised the manuscript; S.W. Qiao, contributed to data acquisition, critically revised the manuscript; Z.S. Shi, contributed to conception and design, data analysis and interpretation, drafted and critically revised the manuscript; X. He, S. Zhu, contributed to conception and design, data acquisition and interpretation, drafted and critically revised the manuscript. All authors gave final approval and agree to be accountable for all aspects of the work.

Supplemental Material

sj-docx-1-jdr-10.1177_00220345251381633 – Supplemental material for Multifunctional Primer for Dentin Bonding via Biomimetic Mineralization

Supplemental material, sj-docx-1-jdr-10.1177_00220345251381633 for Multifunctional Primer for Dentin Bonding via Biomimetic Mineralization by S.H. Yang, Z.L. Tian, H.M. Wang, D. Sun, S.W. Qiao, Z.S. Shi, X. He and S. Zhu in Journal of Dental Research

Footnotes

Declaration of Conflicting Interests

The authors declared no potential conflicts of interest with respect to the research, authorship, and/or publication of this article.

Funding

The authors disclosed receipt of the following financial support for the research, authorship, and/or publication of this article: This work was supported by National Nature Science Foundation of China (82071163). The authors thank State Key Lab of Supramolecular Structure and Materials for the devices and guidance.

ORCID iDs

S.H. Yang

Z.L. Tian

S.W. Qiao

Z.S. Shi

S. Zhu

A supplemental appendix to this article is available online.

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