Effect of Demineralized Dentin Treatment With Tannic Acid for Stabilizing the Resin-Dentin Interface.
Objectives: To evaluate the effect of dentinal treatment with 10% and 20% Tannic Acid (TA), and an adhesive enriched with TA on demineralized coronal dentin for stabilizing the resin-dentin bonding interface. Methods: Middle dentin blocks obtained from human third molars were used to determine the collagen cross-linking capacity of dentin using the hydroxyproline (HYP) release assay. The test groups included: demineralized dentin control with 10% phosphoric acid for 5 hours; vehicle control, 100% ethanol; cross-linking control, 1% glutaraldehyde; adhesive control, Single Bond Universal adhesive; and as experimental groups, 10% and 20% TA; and adhesive enriched with 20% TA. Additionally, the inhibitory capacity of dentin-treated matrix metalloproteinase (MMP) activity was evaluated using a fluorometric assay, and the effect of treatments on microtensile bond strength to demineralized dentin was assessed immediately and after 10,000 cycles of thermocycling using the Shimadzu universal testing machine at a crosshead speed of 0.5 mm/min. Data analysis was performed using the Shapiro-Wilk test, one-way ANOVA, and Tukey's post-hoc test with p ≤ 0.05. Results: Treatment with 10% and 20% TA and with adhesive mixed with TA decreased HYP release. The MMP activity fluorometric assay showed effective inhibition of MMPs in demineralized dentin through TA application. The immediate microtensile bond strength values and those after 10,000 cycles of thermocycling were maintained with dentinal pretreatment with TA at both concentrations and with the TA-enriched adhesive. Conclusions: TA and TA-enriched adhesive demonstrated efficacy as collagen cross-linking agents and inhibitors of MMP activity. These effects resulted in a significant improvement in the stability of the adhesive interface. Moreover, microtensile bond strength values, even after thermal aging, support the effectiveness of TA in promoting bond durability. TA's cross-linking properties help maintain the integrity of collagen fibrils within the dentin matrix, reducing degradation, and enhancing mechanical properties.