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    Experimental, density functional theory, molecular docking and ADMET analyses on the role of different plant extracts of Aronia melanocarpa (Michx) Elliot species on acetylcholinesterase enzyme activity
    (Elsevier, 2025) Gurer, Eda Sonmez; Yildirim, Suheda; Kocyigit, Umit M.; Berisha, Avni; Kaya, Savas
    In the present study, different extracts obtained in different solvents from the fruits collected from the Aronia melanocarpa (Michx.) were prepared. The inhibition performances of these extracts on the inhibition of the acetylcholinesterase enzyme were checked via both theoretical and experimental analyses. Although all extracts used in experimental studies showed high inhibitory activity, it was observed that the extract obtained in methanol had higher inhibitory activity than the others. According to the enzyme activity results presented in the light of Ellman method, IC50 values were found between 0.0311-0.0857 mg/mL. Conceptual Density Functional Theory (CDFT) and Molecular Docking calculations were performed to identify the component or components of the extract with high inhibitory activity. Conceptual Density Functional Theoretical based data commented through popular electronic structure principles such as Maximum Hardness and Minimum Electrophilicity Principles showed that the most reactive one among studied dominant components of the extract is Malvin molecule. The interactions between studied molecules and AChE and mechanisms of these interactions were illuminated via Molecular Docking analyses and ADMET studies. As a result, it was shown that the most reactive molecule Malvin (with lowest hardness and the highest electrophilicity) interacts more powerful with AChE compared to other molecules. Within the framework of the theoretical analyses made, it was proposed that in the design and introduction of new AChE inhibitors, structures with low hardness and high electrophilicity values should be preferred.
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    New Thiazole Derivatives: Carbonic Anhydrase I-II and Cholinesterase Inhibition Profiles, Molecular Docking Studies
    (Wiley-V C H Verlag Gmbh, 2024) Karakaya, Abdullatif; Ercetin, Tugba; Yildirim, Suheda; Kocyigit, Umit M.; Rudrapal, Mithun; Rakshit, Gourav; Cevik, Ulviye Acar
    Thiosemicarbazone derivative was obtained by the addition of thiosemicarbazide to 5-nitro-thiophene-2-carbaldehyde. The addition-cyclization of the 2-bromoacetophenone derivative to thiosemicarbazone derivative gave the new thiazole derivatives (2 a-k). Acetylcholinesterase (AChE), butyrylcholinesterase (BChE), antioxidant, and human carbonic anhydrase (hCA) I and II isoform inhibitory activities of the thiazole derivatives 2 a-k were investigated. The effects of thiazole derivatives on carbonic anhydrase I and II (hCA I-II) isoenzymes were examined in vitro using the esterase method. IC50 values for enzyme inhibition were found to be 2.661-22.712 mu M for hCA I and 5.372-26.813 mu M for hCA II. All derivatives reduced the activities of carbonic anhydrase I and II isoenzymes and were new potential inhibitor molecule candidates. These compounds were found to have minimal effects on AChE and BChE. The antioxidant properties of the target compounds were determined using DPPH and ferric ion-chelating assays. In particular, compounds 2 k and 2 h had the highest antioxidant effect in the series with IC50 values of 30.11 +/- 0.008 mu M and 30.21 +/- 0.006 mu M, respectively. ADMET properties of the compounds found to be effective were evaluated and their interactions with the enzyme were determined by molecular docking.
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    Novel Aminothiazole-Chalcone Analogs: Synthesis, Evaluation Acetylcholinesterase Activity, In Silico Analysis
    (Wiley-V C H Verlag Gmbh, 2025) Sarikaya, Meryem Kececi; Yildirim, Suheda; Kocyigit, Umit M.; Ceylan, Mustafa; Yirtici, Umit; Eyupoglu, Volkan
    In this study, novel thiazole-chalcone analogs were synthesized, and their inhibitory effects on acetylcholinesterase (AChE) were examined. In vitro enzyme activity studies were conducted to calculate IC50 values, which were found to range between 2.55 and 72.78 mu M (tacrine IC50 = 53.31 mu M). The Ki values of the compounds showing the best inhibition (6g and 6e) were calculated and compared to those of the standard substance tacrine. All compounds reduced the AChE activity. Additionally, predictions made with SwissADME indicated that all compounds complied with Lipinski's rules and possessed good oral bioavailability properties, and the inhibitory effects of compounds 6e and 6g on AChE were evaluated using molecular docking and molecular dynamics simulations (100 ns). The results showed that compounds 6e and 6g had strong and stable interactions with AChE.