Publicação
Methacrylated epigallocatechin gallate functionalized dental adhesives: antiproteolytic activity and dentin bonding studies
| dc.contributor.author | Duque, Cristiane | |
| dc.contributor.author | Chrisostomo, Daniela Alvim | |
| dc.contributor.author | Scaffa, Polliana Mendes Candia | |
| dc.contributor.author | Gouveia, Zach | |
| dc.contributor.author | Nascimento, Fabio Dupart | |
| dc.contributor.author | Plotnikov, Sergey V. | |
| dc.contributor.author | Prakki, Anuradha | |
| dc.date.accessioned | 2025-08-14T07:42:03Z | |
| dc.date.available | 2025-08-14T07:42:03Z | |
| dc.date.issued | 2025-07-01 | |
| dc.description.abstract | Objectives: To assess the antiproteolytic effect of EGCG-methacrylate monomers and its inhibitory effect on gelatinolytic activity in the hybrid layer. Also, to investigate the effect of an adhesive material functionalized with EGCG-methacrylate monomers on immediate and long-term dentin-resin bond strength. Methods: Neat EGCG (E0) was reacted with three different ratios of methacryloyl ester and dissolved in ethyl acetate to obtain EGCG-methacrylates with hydroxyl functionalization at 33 % (M-E33), 67 % (M-E67) and 100 % (M-E100) levels. Resin composite blocks were built on human dentin surfaces using self-etching adhesive containing E0, M-E33, M-E67, and M-E100 at 1 wt%. Demineralized human dentin disks were immersed in deionized water (DW) or lactic acid (LA) and subsequently treated with DW, acetone (as controls), E0, M-E33, M-E67 and M-E100 diluted in acetone. Concentrations of solubilized type I collagen C-terminal (CTX and ICTP) and N-terminal (NTX) telopeptides were determined from 7-day extracts of dentin matrix specimens by ELISA assays. In situ zymography of adhesive-dentin interface slices from restored teeth was performed by confocal microscope after 24 h dentin treatment. Microtensile bond strength (µTBS) and failure pattern were evaluated after 24 h and 6 months. Data were analyzed using two-way ANOVA and Tukey post hoc test (p < 0.05). Results: All experimental groups statistically reduced the release of solubilized telopeptides from dentin samples in DW and LA. E0 and M-E100 incorporated into the adhesive system reduced the gelatinolytic activity within the hybrid layer. The lowest µTBS values for restored teeth were observed for E0 and M-E100 groups, after 24 h and 6 months, respectively. The most prevalent failure observed was classified as type 4, except for M-E100. Significance: EGCG-methacrylate monomers effectively protected collagen from degradation. When incorporated into adhesive systems, EGCG-methacrylates reduced gelatinolytic activity within the hybrid layer, and did not affect immediate and long-term bond strength values of restorations. | eng |
| dc.identifier.citation | Duque, C., Chrisostomo, D. A., Scaffa, P. M. C., & Gouveia, Z. et al. (2025). Methacrylated epigallocatechin gallate functionalized dental adhesives: antiproteolytic activity and dentin bonding studies. Dental Materials, 41(7), 892-900. https://doi.org/10.1016/j.dental.2025.05.006 | |
| dc.identifier.doi | 10.1016/j.dental.2025.05.006 | |
| dc.identifier.eid | 105007063167 | |
| dc.identifier.issn | 0109-5641 | |
| dc.identifier.other | 282764be-8b5c-47c8-aa86-f86a65de024d | |
| dc.identifier.pmid | 40467428 | |
| dc.identifier.uri | http://hdl.handle.net/10400.14/54574 | |
| dc.identifier.wos | 001508912600010 | |
| dc.language.iso | eng | |
| dc.peerreviewed | yes | |
| dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | |
| dc.subject | Adhesives | |
| dc.subject | EGCG | |
| dc.subject | Human dentin | |
| dc.subject | Metalloproteinases | |
| dc.subject | Methacrylates | |
| dc.title | Methacrylated epigallocatechin gallate functionalized dental adhesives: antiproteolytic activity and dentin bonding studies | eng |
| dc.type | research article | |
| dspace.entity.type | Publication | |
| oaire.citation.endPage | 900 | |
| oaire.citation.issue | 7 | |
| oaire.citation.startPage | 892 | |
| oaire.citation.title | Dental Materials | |
| oaire.citation.volume | 41 | |
| oaire.version | http://purl.org/coar/version/c_970fb48d4fbd8a85 |
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