Ellagic acid on the quality of the adhesive interface of class I composite resin restorations after aging
DOI:
https://doi.org/10.14393/BJ-v38n0a2022-61206Palavras-chave:
Dental adhesives, Ellagic acid, Microscopy, Electron, Scanning Transmission.Resumo
Objective: To evaluate the effect of ellagic acid on the inhibition of matrix metalloproteinase by analyzing the quality of the adhesive interface with bond strength measures in periods of 24 hours and six months of storage. Method: 40 healthy human third molars were prepared with class I cavities (5x4x3mm). The teeth were divided into four experimental groups: Group 1- without application of ellagic acid and storage time of 24 hours; Group 2- with ellagic acid/24 hours; G3- without ellagic acid/six months; Group 4- with ellagic acid/six months. Then, the cavities were restored with Single Bond Universal adhesive and Z350 composite resin, with and without the previous application of ellagic acid. Subsequently, hourglass-shaped specimens were obtained and subjected to the bond strength (BS) test (n = 10) in a universal testing machine. The bond test was performed after 24 hours and six months of storage. For the standard evaluation (n = 3) the samples were infiltrated with silver nitrate and placed in a developing solution for analysis in a Scanning Electron Microscope (SEM). The data obtained were analyzed with the Kruskal-Wallis non-parametric test, showing a statistically significant difference. Results: The highest bond strength values were found for the 24-hour groups followed by the groups with six months of storage. For nano-infiltration, groups G1 and G2 showed lower infiltration than groups G3 and G4. Conclusion: The previous application of ellagic acid did not affect the BS of the adhesive interface of the adhesive system analyzed, regardless of storage time.
Downloads
Referências
BOELEN, G.J., et al. Matrix metalloproteinases and inhibitors in dentistry. Clinical Oral Investigations. 2019, 23(7), 2823-2835. https://doi.org/10.1007/s00784-019-02915-y
BRESCHI, L., et al. Dentin bonding systems: From dentin collagen structure to bond preservation and clinical applications. Dental Materials. 2018, 34(1), 78-96. https://doi.org/10.1016/j.dental.2017.11.005
FERDOSIAN, F., et al. Bio-Based Adhesives and Evaluation for Wood Composites Application. Polymers (Basel). 2017, 9(2), 70. https://doi.org/10.3390/polym9020070
FISCHER, T., SENN, N., and RIEDL, R. Design and Structural Evolution of Matrix Metalloproteinase Inhibitors. Chemistry. 2019, 25(34), 7960-7980. https://doi.org/10.1002/chem.201805361
HASS, V., et al. Is it possible for a simultaneous biomodification during acid etching on naturally caries-affected dentin bonding? Clinical Oral Investigations. 2021, 25(6), 3543-3553. https://doi.org/10.1007/s00784-020-03677-8
KONG, W. J., GU, X. H., and SUN, J. Progress in biomodification of dentin type Ⅰ collagen by different types of cross-linkers. Zhonghua Kou Qiang Yi Xue Za Zhi. 2020, 55(2), 135-138. https://doi.org/10.3760/cma.j.issn.1002-0098.2020.02.013
MAZZONI, A., et al. Zymographic analysis and characterization of MMP-2 and -9 forms in human sound dentin. Journal of Dental Research. 2007, 86(5), 436-440.
MAZZONI, A., et al. MMP activity in the hybrid layer detected with in situ zymography. Journal of Dental Research. 2012, 91(5), 467-72.
MAZZONI, A., et al. Effects of Etch-and-Rinse and Self-etch Adhesives on Dentin MMP-2 and MMP-9. Journal of Dental Research. 2013, 92(1), 82–86. https://doi.org/10.1177%2F0022034512467034
MARAVIC, T., et al. How Stable is Dentin As a Substrate for Bonding? Current Oral Health Reports. 2017, 4(3), 248–257. https://doi.org/10.1007/s40496-017-0149-8
NISHITANI, Y., et al. Activation of gelatinolytic/collageno- lytic activity in dentin by self-etching adhesives. European Journal of Oral Sciences. 2006, 114(2), 160-6. https://doi.org/10.1111/j.1600-0722.2006.00342.x
OSORIO, R., et al. Effect of dentin etching and chlorhexidine application on metalloproteinase-mediated collagen degradation. European Journal of Oral Sciences. 2011, 119(1), 79-85. https://doi.org/10.1111%2Fj.1600-0722.2010.00789.x
OU, Q., et al. Effect of matrix metalloproteinase 8 inhibitor on resin-dentin bonds. Dental Materials. 2018, 34(5), 756-763. https://doi.org/10.1016/j.dental.2018.01.027
PERDIGÃO, J., et al. Adhesive dentistry: Current concepts and clinical considerations. Journal of Esthetic and Restorative Dentistry. 2021, 33(1), 51-68. https://doi.org/10.1111/jerd.12692
SCAFFA, P.M.C., et al. Co-distribution of cysteine cathepsins and matrix metalloproteases in human dentin. Archives of Oral Biology. 2017, 74, 101–107. https://doi.org/10.1016/j.archoralbio.2016.11.011
SHAVANDI, A., et al. Polyphenol uses in Biomaterials Engineering. Biomaterials. 2018, 167, 91–106. https://doi.org/10.1016/j.biomaterials.2018.03.018
TREVELIN, L.T., et al. Effect of dentin biomodification delivered by experimental acidic and neutral primers on resin adhesion. Journal of Dentistry. 2020, 99, 103354. https://doi.org/10.1016/j.jdent.2020.103354
TJÄDERHANE, L., et al. Dentin basic structure and composition—an overview. Endodontic Topics. 2012, 20(1), 3-29. https://doi.org/10.1111/j.1601-1546.2012.00269.x
TJÄDERHANE, L., et al. Optimizing dentin bond durability: control of collagen degradation by matrix metalloproteinases and cysteine cathepsins. Dental Materials. 2013, 29(1), 116–135. https://doi.org/10.1016/j.dental.2012.08.004
ZHANG, S.C., and KERN, M. The Role of Host-derived Dentinal Matrix Metalloproteinases in Reducing Dentin Bonding of Resin Adhesives. International Journal of Oral Sciences. 2009, 1(4), 163–176. https://doi.org/10.4248/ijos.09044
ZHOU, W., et al. Modifying Adhesive Materials to Improve the Longevity of Resinous Restorations. International Journal of Molecular Sciences. 2019, 20(3), 1-20. https://doi.org/10.3390/ijms20030723
Downloads
Publicado
Como Citar
Edição
Seção
Licença
Copyright (c) 2022 Josué Junior Araújo Pierote, Lucia Trazzi Prieto, Júlia Marques Pires, João Victor Frazão Câmara, Cíntia Tereza Pimenta de Araújo, Isabel Ferreira Barbosa, Gisele Damiana da Silveira Pereira, Justine Monteiro Monnerat Tinoco, Renato Feres de Carvalho Vianna, Hana Fried, Sonia Groisman, Luis Alexandre Maffei Sartini Paulillo
Este trabalho está licenciado sob uma licença Creative Commons Attribution 4.0 International License.