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Öğe Design, synthesis and molecular modeling studies of thiosemicarbazide & thiazolyl-hydrazone derivatives as potential anticancer agents and topoisomerase inhibitors(Elsevier, 2024) Senkardes, Sevil; Bolat, Irfan; Sahinbey, Hazal; Karakus, Sevgi; Erdogan, Omer; Canturk, Pakize; Ozguven, Serap YilmazThis study involved the design, synthesis and evaluation of a series of novel thiosemicarbazide and thiazolylhydrazone derivatives. The synthesized compounds were tested for cytotoxic effects SH-SY5Y neuroblastoma cells, as well as NIH-3T3 normal cell line using the MTT assay. Among the tested compounds, 3b, 3d, 3i, 4b, 4d and 4i exhibited IC50 values ranging from 1.97 mu M to 3.22 mu M in the SH-SY5Y cancer cell line with lower cytotoxicity toward NIH-3T3 cells. Moreover, all compounds were also screened for their topoisomerase I and II inhibitory activity and compound 3b completely inhibited the topoisomerase I enzyme, whereas all compounds showed potent topoisomerase II inhibitory activity. Docking studies were performed to identify the mode of binding of the tested compounds to the active site of topoisomerase I and II. In conclusion, N-(4-(2-((2-chlor- ophenyl)carbamothioyl)hydrazine-1-carbonyl)phenyl)benzamide (3b) emerges as a promising inhibitor of topoisomerase I and II and holds potential as a lead compound in the quest for novel anticancer agents.Öğe Enzyme inhibitory potential of some indole Schiff bases on acetylcholinesterase and human carbonic anhydrase isoforms I and II enzymes: an in vitro and molecular docking study(Taylor & Francis Inc, 2023) Akman, Ebru; Sirinzade, Hanif; Ozguven, Serap Yilmaz; Dilek, Esra; Suzen, SibelIn this study, the in vitro effects of some indole Schiff bases on acetylcholinesterase and human carbonic anhydrase isoforms I and II were investigated. A series of N-methylindole hydrazide/hydrazone derivatives (1a-1t) were tested on these enzymes. The interactions of the synthesized indole derivatives with target enzymes were studied by molecular docking methodology. The results revealed that indole derivative Schiff base compounds inhibited the enzymes significantly. Ki values for hCAI isoenzyme were determined to be in the range of 36.18 +/- 3.07-224.29 +/- 5.78 nM; for the hCAII isoenzyme in the range of 31.30 +/- 2.63-201.64 +/- 7.25 nM; for acetylcholinesterase in the range of 6.82 +/- 0.72-110.30 +/- 9.26 nM. Compared to the control compound Acetazolamide (AZA), 1k and 1p were found to have the best inhibitory effect for hCAI; 1p was found to be the best inhibitory effect for hCAII. Compared to the control compound Tacrine (TAC), 1s showed the best inhibitory effect for AChE. In vitro results were verified with the results obtained by docking studies and interactions with enzymes were demonstrated.{GRAPHIACAL ABSTRACT}Öğe Investigation of inhibition kinetics of various plant extracts on polyphenol oxidase enzyme from Paulownia Tomentosa and binding mechanism by molecular docking(Elsevier, 2024) Cesko, Cengiz; Arabaci, Gulnur; Paluzar, Hatice; Ozguven, Serap YilmazPolyphenol oxidase/tyrosinase enzyme, which contains binuclear copper clusters play an important role in melanogenesis and enzymatic browning. Therefore, its inhibitors can be attractive in cosmetics and medicinal industries as depigmentation agents and also in food and agriculture industries as antibrowning compounds. Our aim in this study is to find natural plant extracts that will inhibit the polyphenol oxidase enzyme. The inhibitory effects of Verbascum thapsus, Tanacetum vulgare, Solanum nigrum and Datura stramonium herbal plant extracts obtained from Kosovo on the polyphenol oxidase enzyme activity were investigated. Polyphenol oxidase from the Poulownia tomentosa plant was purified using the three-phase purification method. It is determined that T. vulgare extract showed the most effective inhibitory effect with 0.43 mg/mL IC50 value. In order to explain and support the binding mechanism of the best inhibitor extract, the phenolic content of the T. vulgare extract was determined by LC-MS/MS and the mechanism of the inhibitory effect was explained by performing a molecular docking study for the phenolic compounds it contained at the highest rate.Öğe Synthesis, Characterization, Molecular Docking Studies and Biological Evaluation of Some Novel 3,5-disubstituted-1-phenyl-4,5-dihydro-1H-pyrazole Derivatives(Bentham Science Publ Ltd, 2024) Tok, Fatih; Bayrak, Ilayda Rumeysa; Karakaraman, Elif; Soysal, Irem; Cakir, Cansel; Tuna, Kubra; Ozguven, Serap YilmazIn this study, some new pyrazoline derivatives bearing cyano or nitro groups were synthesized. The structures of the compounds were characterized by IR, H-1-NMR, C-13-NMR and elemental analysis data. The ABTS(+), DPPH, CUPRAC and beta-Carotene/linoleic acid assays were carried out to determine the antioxidant activity of the synthesized pyrazolines. Compound P14 showed higher antioxidant activity than the standard substance BHA with IC50 values of 1.71 +/- 0.31 mu M and 0.29 +/- 0.04 mu M in ABTS(+) and beta-carotene/linoleic acid assays, respectively. Compound P12 also exhibited higher antioxidant activities than BHA with an IC50 value of 0.36 +/- 0.14 mu M in beta-carotene/linoleic acid analysis. In activity studies of pyrazolines against cholinesterase (AChE and BChE), tyrosinase, alpha-amylase and alpha- glucosidase, compound P1 (IC50 = 39.51 +/- 3.80 mu M) showed higher activity against alpha-amylase and compounds P5 and P12 displayed higher activity against alpha-glucosidase than acarbose with IC50 values of 14.09 +/- 0.62 and 83.26 +/- 2.57 mu M, respectively. The drug-like properties such as Lipinski and Veber, bioavailability and toxicity risks of the synthesized compounds were also evaluated. The compounds were predicted to be compatible with Lipinski and Veber rules, have high bioavailability and low toxicity profiles. Moreover, molecular docking studies were performed to better understand the high activity of the compounds against a-amylase and a-glucosidase enzymes.
