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    Activities of New Dinuclear PEPPSI-Precatalysts Bearing Bis-benzimidazole Ligands in the Suzuki-Miyaura Coupling Reaction
    (Wiley-V C H Verlag Gmbh, 2026) Yilmaz, Ulku; Gok, Yetkin; Aktas, Aydin
    Seven new PEPPSI (Pyridine-Enhanced Precatalyst Preparation Stabilization and Initiation) type complex compounds containing bisbenzimidazole ligands were synthesized, and their structures were characterized by spectroscopic methods (1H, 13C-NMR, IR, HRMS). The catalytic activities of PEPPSI-precatalysts were tested in Suzuki-Miyaura cross-coupling reactions using phenylboronic acid, aryl bromides and aryl chlorides. It was observed that the precatalysts, having electron-dense benzimidazole ligands (compounds 1, 2), exhibited higher catalytic activity. In contrast, catalyst precursors having electron-poor benzimidazole ligands were found to have lower catalytic activity (compound 7).
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    Bisbenzimidazole salts and their in silico-in vitro inhibitory abilities on hCA I, hCA II, and AChE enzymes
    (Springer Wien, 2024) Yilmaz, Ulku; Demir, Yeliz; Tok, Tugba Taskin; Gok, Yetkin; Aktas, Aydin; Gulcin, Ilhami
    Eight new bisbenzimidazolium halides were prepared from alkyl halides and 4,4 '-bis[(benzimidazol-1-yl)methyl]-1,1 '-biphenyl.The structures of the benzimidazole salts were characterized using elemental analysis techniques as well as 1H, 13C NMR, and FT-IR spectroscopic methods. The inhibitory effects of the benzimidazole derivatives were measured against human carbonic anhydrase I (hCA I), human carbonic anhydrase II (hCA II), and acetylcholinesterase (AChE) enzymes. All benzimidazolium halides exhibited significant enzyme inhibitory properties. They showed highly potent inhibitory effect on AChE and hCAs (Ki values are in the range of 15.7 +/- 0.8 to 49.7 +/- 10.1 nM, 14.6 +/- 1.5 to 70.7 +/- 2.7 nM, and 17.4 +/- 2.8 to 38 +/- 10 nM for AChE, hCA I, and hCA II, respectively). The binding orientation of the synthesized bisbenzimidazolium halides was evaluated by molecular docking studies, reflecting the importance of the p-methylbenzyl, m-methylbenzyl, p-nitrophenethyl, and 3-(1,3-dioxoisoindolin-2-yl)methyl) groups in protein-ligand interaction. The docking results support the Ki values of the respective compounds in this study. The structure-activity relationships against the various targets are clearly shown in three dimensions at the atomic level by their interactions with the mentioned enzymes.