Aim: Compositional modification of conventional glass ionomer luting cements by incorporating two types of all-ceramic powders in varying concentrations and evaluation of their film thickness, setting time, and strength. Material & Methods. Experimental GICs were prepared by adding different concentrations of two all-ceramic powders (5%, 10, and 15% by weight) to the powder of the glass ionomer luting cements, and their setting time, film thickness, and compressive strength were determined. The Differential Scanning Calorimetry analysis was done to evaluate the kinetics of the setting reaction of the samples. The average particle size of the all-ceramic and glass ionomer powders was determined with the help of a particle size analyzer.
Results: A significant increase in strength was observed in experimental GICs containing 10% all-ceramic powders. The experimental GICs with 5% all-ceramic powders showed no improvement in strength, whereas those containing 15% all-ceramic powders exhibited a marked decrease in strength. Setting time of all experimental GICs progressively increased with increasing concentration of all-ceramic powders. Film thickness of all experimental GICs was much higher than the recommended value for clinical application.
Conclusion: 10% concentration of the two all-ceramic powders can be regarded as the optimal concentration for enhancing the glass ionomer luting cements' strength. There was a significant increase in the setting time at this concentration, but it was within the limit specified by ISO 9917-1:2007 specifications for powder/liquid acid-base dental cements. Reducing the particle size of the all-ceramic powders may help in decreasing the film thickness, which is an essential parameter for the clinical performance of any luting cement.
Natural products such as essential oils (EOs) are secondary metabolites that can be obtained from either plant or animal sources or produced by microorganisms. Much attention has been given to exploring the use of secondary metabolites as natural antibacterial agents. This study investigates the antibacterial activity and mechanism of β-caryophyllene, a compound that can be found in various EOs, against Bacillus cereus. The minimum inhibitory concentration of β-caryophyllene against B. cereus was 2.5% (v/v), whereas killing kinetics of β-caryophyllene at minimum inhibitory concentration recorded complete bactericidal activity within 2 hours. Zeta-potential measurement in the cells treated with half the minimum inhibitory concentration of β-caryophyllene at 1.25% (v/v) showed an increase in the membrane permeability surface charge to –3.98 mV, compared to untreated cells (–5.46 mV). Intracellular contents leakage of UV-absorbing materials was detected in the cells treated with β-caryophyllene. Additionally, β-caryophyllene does not interfere with the efflux activity of B. cereus via the ethidium bromide influx/efflux activity. The results revealed that β-caryophyllene was able to alter membrane permeability and integrity of B. cereus, leading to membrane damage and intracellular content leakage, which eventually caused cell death.
METHODS: The three variants expressed by bacteria were investigated using substrate (omeprazole and 3- cyano-7-ethoxycoumarin[CEC]) and inhibitor (ketoconazole, fluoxetine, sertraline and loratadine) probes in enzyme assays along with molecular docking.
RESULTS: All alleles exhibited very low enzyme activity and affinity towards omeprazole and CEC (6.1% or less in intrinsic clearance). The inhibition studies with the four inhibitors, however, suggested that mutations in different variants have a tendency to cause enhanced binding (reduced IC50 values). The enhanced binding could partially be explained by the lower polar solvent accessible surface area of the inhibitors relative to the substrates. Molecular docking indicated that G91R, R335Q and F448L, the unique mutations in the alleles, have caused slight alteration in the substrate access channel morphology and a more compact active site cavity hence affecting ligand access and binding. It is likely that these structural alterations in CYP2C19 proteins have caused ligand-specific alteration in catalytic and inhibitory specificities as observed in the in vitro assays.
CONCLUSION: This study indicates that CYP2C19 variant selectivity for ligands was not solely governed by mutation-induced modifications in the active site architecture, but the intrinsic properties of the probe compounds also played a vital role.