Browsing by Author "Oguz, E."

Now showing 1 - 2 of 2

Design, Synthesis, and AChE Inhibition of 4-Amino Derivatives: Molecular Docking and Biological Evaluation
(Pleiades Publishing Ltd, 2025) Oguz, E.; Cetin, A.; Kazancioglu, M. Z.; Kazancioglu, E. A.; Turkan, F.
Substituted tetrahydroquinoline (THQ) derivatives were systematically designed and synthesized via a three-component Povarov reaction, employing N-vinyl carbamate, organocatalyzed substituted anilines, and benzaldehyde derivatives. The resulting THQ derivatives demonstrated a diverse range of functional groups, which potentially broadens their applicability. These compounds were rigorously characterized using various spectroscopic techniques to verify their structures. Subsequent bioevaluation of the synthesized THQs revealed their inhibitory activity against acetylcholinesterase (AChE), highlighting their potential as therapeutic agents for neurodegenerative diseases. All synthesized THQs exhibited IC50 values ranging from 0.22 to 0.36 mu M, which are lower than the IC50 value of the standard compound tacrine (0.77 mu M). The Ki values for the THQs against AChE ranged from 0.370 +/- 0.330 to 1.30 +/- 0.715 mu M. Additionally, molecular docking studies of the THQ-AChE complexes yielded binding scores between -10.8 and -12.4 kcal/mol. The structure-activity relationship (SAR) analysis underscores the significance of THQ structures in medicinal chemistry. These findings suggest that the structural insights gained from this study will be valuable for the future design and synthesis of potent AChE inhibitors.
In Silico and In Vitro Analysis of Acetylcholinesterase and Glutathione S-Transferase Enzymes of Substituted Pyrazoles
(Maik Nauka/interperiodica/springer, 2022) Cetin, A.; Oguz, E.; Tuerkan, F.
A series of substitute pyrazole compounds including azide, acetyl, triazole, morpholine, piperidine, and pyrrolidine moieties were synthesized and their structures were elucidated by NMR, HPLC and mass spectroscopy. The inhibition efficiencies of all novel compounds against acetylcholinesterase (AChE) and glutathione S-transferase (GST) enzymes were investigated. In vitro studies revealed that the inhibitory activities of substitute pyrazole compounds were determined with Ki values in the range of 0.11-0.49 mu M for AChE, and 0.12-0.91 mu M for GST, respectively. Furthermore, the molecular docking studies of the detailed interactions between the pyrazole compounds and AChE-GST enzymes were identified with bonding type, distance, hydrophobic bonds and hydrogen bonds. The binding energies of the AChE-pyrazole analogs' complexes were found between -5.5 and - 9.3 kcal/mol, and the binding energies of the GST-pyrazole analogs' complexes were found between -5.9 and - 9.2 kcal/mol.