The Effect of Matrix Metalloproteinase Inhibitors on the Microtensile Bond Strength of Dentin Bonding Agents in Caries Affected Dentin: A Systematic Review.

Aims and Objectives: Matrix metalloproteinases (MMPs) cause degradation of the dentinal matrix, as they act actively on collagen fibrils, leading to their deterioration and collapse. MMP inhibitors are known to be used for the pre-treatment of human dentin before bonding. Most studies on the MMP inhibitors examined the effect of MMP inhibitors on bonding to sound dentin (SD), but few examine their effect on bonding to caries affected dentin (CAD). This systematic review aims to identify and summarize studies that have applied MMP inhibitors for pre-treatment of CAD, and examine the microtensile bond strength (µTBS), bond durability, and the mode of failure. Materials and Methods: A systematic review was performed using the PubMed database according to the PRISMA guidelines. A total of 785 original articles published between 2010 and 2022 were initially retrieved. Six studies were selected based on predefined inclusion-exclusion criteria, and their outcomes were extracted and analyzed. The methodological quality assessment was performed using a combined checklist that utilizes the reporting criteria mentioned in the checklist for reporting in-vitro studies guidelines and guidelines for reporting pre-clinical in vitro studies on dental materials. Results: All six studies included here showed a definitive increase of the µTBS when MMP inhibitors were applied to the CAD. The mode of failure was found to be predominantly adhesive in nature. The deviation in the values of µTBS was approximately 2-5 MPa on immediate and delayed testing. Conclusion: MMP-inhibiting agents could be considered for the pretreatment of teeth with CAD as a part of their tooth preparation area, thereby allowing the clinician to retain CAD and bond to the CAD without endangering the vital pulp.

Reinforcing an immature tooth model using three different restorative materials.

Background: To compare and evaluate the strength rendering capacity of three restorative materials in tooth model simulated as immature teeth. Materials and Methods: In this in vitro study, 80 human maxillary permanent central incisors scheduled for periodontal extraction were collected, and an immature tooth model was prepared using a 3 mm twist drill. To simulate single-visit apical barrier, all the teeth were prepared with peso number 1-6. The teeth were segregated into three experimental and a control group. The experimental groups (n = 20) comprised of fiber-reinforced composite (FRC), Biodentine, and glass ionomer cement. The fracture resistance of all the teeth was tested using universal testing machine. The final reading of the applied load to cause fracture was noted and later was subjected to statistical analysis, P ≤ 0.05 was considered statistically significant, and the level of significance was fixed at 5%. Student's t-test was applied to compare values among experimental groups. Results: There was a significant difference in the values of peak load resulting in fracture among experimental groups which was observed statistically (P ≤ 0.001). FRC exhibited superior reinforcing capacity (mean: 1199.7 N) among the experimental materials followed by Biodentine and Bioglass R. The lowest value to fracture was observed in control group (mean: 236.7 N). Conclusion: The results indicate that FRC could substantially contribute positively in reinforcing the simulated thin-walled immature roots.

Kinetic studies on thermal denaturation of C-phycocyanin.

The kinetics of thermal denaturation of a biliprotein, C-phycocyanin (C-PC) isolated from Spirulina platensis were studied at different pH values, ranging from 4.0 to 8.0. The denaturation of C-PC follows the first order kinetics and rate constant at pH 5.0 and temperature 55 degrees C is found to be 4.37 x 10(-5) s(-1), which increases to 5.46 x 10(-1) s(-1) at pH 7.0. The denaturation rate is much higher at 65 degrees C and pH 7.0 (7.96 x 10(-4)), as compared to at pH 5.0 (1.46 x 10(-4)). The thermal stability of C-PC is more at pH 5.0, as compared to other pH values. The observed differences in entropy values at pH 5.0, as compared to other pH values indicate a considerably close fit structure of the protein at pH 5.0, which increases the stability of native structure, even at higher temperature (65 degrees C).