This study aims to examine the effect of a-tomatine, a new matrix metalloproteinase inhibitor for dentistry, as a surface pretreatment on the bonding strength of different types of dentine via in vitro and in silico methods. The binding efficacy of both a-tomatine and chlorhexidine to MMP-2, 8, and 9 was evaluated through molecular docking and dynamics analyses. For microtensile testing (µTBS), specimens (n = 84) were categorized into two groups based on the type of dentin: sound (SD) and eroded (ED) (n = 42). Each group was further divided into three subgroups according to the utilization of surface pretreatment agents (1.5 µM of tomatine, 2% chlorhexidine (CHX), and the control). Composite buildups were gradually created via a three-step etch-and-rinse technique. The specimens were sectioned into sticks and subsequently subjected to µTBS after aging for either 24 h (n = 7) or 6 months (n = 7). The data were subjected to analysis using two-way ANOVA with a Bonferroni correction post hoc test. The significance level was evaluated at a minimum of p < 0.05. According to molecular docking and dynamic simulation analyses, a-tomatine exhibits a higher affinity for MMP-2, -8, and -9 enzymes compared to chlorhexidine. Lower µTBS values were observed in all ED groups compared to the SD groups. Following 24-h aging, the CHX application in both the SD and ED groups achieved lower µTBS values compared to the control group (p < 0.01 and p > 0.05, respectively). The most favorable results were consistently achieved across all the subgroups subjected to a-tomatine applications (p < 0.05). a-tomatine is a more effective MMP inhibitor than chlorhexidine in terms of preserving bond strength values over time and its capacity to bind to MMP-2,8, and 9 for inhibition.

This research aimed to identify potential drug compounds from the ZINC15 molecule database that could effectively treat GnRH1R-related diseases. The study utilized molecular docking and molecular dynamics methods to achieve this goal, which is crucial in drug repurposing research. The virtual screening process involved analyzing known drug compounds using molecular docking. Additionally, molecular dynamics simulations and MM-GBSA were employed to evaluate the stability of the complexes and determine the interactions between the compounds and protein structure. As a result, this study provides significant insights for treating diseases such as endometriosis, uterine fibroids, and prostate cancer related to GnRH1R. The study also involved designing new drugs and identifying necessary molecular scaffolds.

In this study, in vitro enzyme activity assays were performed to investigate the inhibitory effects on α-glucosidase and tyrosinase-related protein 1, while in silico molecular docking, molecular dynamics, and protein dynamics analyses were performed to provide information on molecular mechanisms. According to information obtained from in silico approaches, inhibition properties are responsible for conformational changes in protein structures, occupation of the active site cleft by the dominant compounds in the extract, as well as long-term changes in protein folding due to departure from the usual motion. The IC₅₀ values of Cardaria draba (L.) DESV. subsp. Chalepensis (L.) extract for α-glucosidase and tyrosinase-related protein 1 were determined to 1.89 ± 0.13 µg/ml and 1.53 ± 0.13 µg/ml, respectively. In addition, the IC₅₀ value of the antiproliferative effects of the extract on DLD-1 colon cancer cells was found to be 6.9 µg/mL. Preclinical trials are warranted to validate the extract’s therapeutic potential. These findings suggest that Cardaria draba extract exhibits enzyme inhibitory and antiproliferative properties, warranting further investigation for its potential role in therapeutic interventions. Further research, particularly in vivo studies, is required to explore the potential of this extract to address DLD-1.