Functionalized imidazolium and benzimidazolium salts as paraoxonase 1 inhibitors: Synthesis, characterization and molecular docking studies

Novel N‐propylphthalimide‐ and 4‐vinylbenzyl‐substituted benzimidazole salts: Synthesis, characterization, and determination of their metal chelating effects and inhibition profiles against acetylcholinesterase and carbonic anhydrase enzymes

“…In addition, recently enzyme inhibition studies of NHC ligands such as imidazole, benzimidazole, and imidazolidine have been conducted. NHC ligands have been demonstrated to be highly active in enzyme inhibition studies …”

Association of human serum paraoxonase‐1 with some respiratory drugs

“…However, there are very few studies investigating the interaction between PON activity and pharmaceutical products …”

Inhibition of paraoxonase 1 by coumarin‐substituted N‐heterocyclic carbene silver(I), ruthenium(II) and palladium(II) complexes

“…Aliphatic alcohols, some metal ions, acetylsalicylic acid, coumarin derivatives, anaesthetics, antibiotics, calcium channel blockers, cardiovascular therapeutics, some anticancer agents, some pesticides, some copper complexes, sulfonamide derivatives and antiepileptic drugs have been investigated by various research groups in view of their possible effects on PON1 activity. Additionally, our group investigated the PON1 inhibitory properties of imidazolium salts with coumarin, benzoxazinone or benzotriazole moieties and we showed that coumarin‐substituted imidazolium salts are stronger inhibitors of PON1 than corresponding 4‐chloromethylene coumarins . Therefore, in this study we used coumarin‐substituted benzimidazolium chlorides as NHC precursors.…”

“…A kinetic investigation was performed using 6b and the results showed that this complex inhibits PON1 activity in a non‐competitive manner (Figure ) with K i value of 1.16 (±0.96) μM ( V max = 11.75 μmol min −1 , K m = 53.63 μM). In our previous studies, we reported the inhibitory properties of a series of coumarin‐functionalized azolium salts and those compounds inhibited the activity of PON1 in a competitive manner . The non‐competitive inhibitory profile of 6b can be explained by the increased molecular size and possible interactions with some residues which are not part of the active site but play important roles in activity.…”