30 publications from this institution
Various Nepeta species, widely used among the public, have valuable phytochemical contents and clinical and biological activities. For this reason, our study examined the enzyme inhibition and antibacterial properties of methanol: chloroform (1:1) extracts of six Nepeta species. N. aristata showed a higher inhibitory effect than the standard drug on seven of the eight enzymes studied. N. baytopii had a high inhibition effect on urease and lipase. It was determined that N. italica inhibited other enzymes except for urease, CA, and lipase. In addition, BChE is also the only effective plant. N. nuda subsp. albiflora has a high effect on inhibiting urease, AChE, and lipase. N. stenantha and N. trachonitica also showed inhibition effects on urease, AChE, and tyrosinase. In the disc diffusion method of antibacterial activity, extracts against B. cereus had antibacterial activity. The antimicrobial activity of N. aristata extract was effective against P. aerugonisa and K. pneumoniae. Additionally, when looking at the minimum inhibition concentration method of antibacterial activity, Nepeta extracts were effective against most bacteria. This research determined Nepeta extracts are effective natural products with antioxidant and enzyme inhibition activities.
The acid catalyzed hydrolysis of the N-(p-substitutedphenyl) phthalimides in three different acids was investigated at 50.0 ± 0.1 °C. Two different antioxidant activity tests as DPPH• and ABTS•+ scavenging activities, and three various enzyme inhibition activity tests as urease, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) inhibition activities, were applied. Compound 3c (2.03 μg/mL ) has higher antioxidant activity than other compounds and standards according to DPPH test. In AChE assay, compounds 3a and 3b (13.13 and 9.59 μg/mL) has higher enzyme inhibition activity than the standard Galantamine (14.37 μg/mL). In BChE and urease tests, all compounds (6.84-13.60 and 10.49-17.73 μg/mL) have higher enzyme inhibition activity than the standard Galantamine (49.40 μg/mL) and thiourea (26.19 μg/mL), respectively. The molecule interaction for each of the three compounds with the active sites of AChE, BChE, and urease enzymes was examined via molecular docking simulations.