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    Imidazolinium chloride salts bearing wingtip groups: Synthesis, molecular docking and metabolic enzymes inhibition
    (Elsevier Science Bv, 2019) Yigit, Beyhan; Kaya, Ruya; Taslimi, Parham; Isik, Yilmaz; Karaman, Muhammet; Yigit, Murat; Ozdemir, Ismail
    A series of symmetrical imidazolinium chloride salts bearing secondary N-alkyl substituents were synthesized in good yield by the reaction of N,N'-dialkylethane-1,2-diamines and HC(OEt)(3) in the presence of NH4Cl. These salts were characterized by spectroscopic methods. All compounds were tested as enzyme inhibitory agents. These novel symmetrical imidazolinium chloride salts derivatives (3a-h) effectively inhibited the cytosolic hCA I and hCA II, BChE, alpha-glycosidase and AChE with K-i values in the range of 18.41-121.73 nM for hCA I, 12.50-63.12 nM for hCA II, 3.72-34.58 nM for AChE, 5.50-32.36 nM for BChE, and 94.72-364.51 nM for alpha-glycosidase, respectively. CA isoenzymes play a crucial roles including acid-base balance homeostasis by excreting and secreting protons (H+) due to the CO2 hydration, HCO3- reabsorption mechanisms, and renal NH4+ output. Also, the molecular modeling is an implementation for estimation of the binding proximity of symmetrical imidazolinium chloride salts bearing secondary wingtip groups and their inhibition mechanisms and kinetics in atomic levels at the catalytic domains. (C) 2018 Elsevier B.V. All rights reserved.
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    Novel 2-aminopyridine liganded Pd(II) N-heterocyclic carbene complexes: Synthesis, characterization, crystal structure and bioactivity properties
    (Academic Press Inc Elsevier Science, 2019) Erdemir, Pato; Celepci, Duygu Barut; Aktas, Aydin; Gok, Yetkin; Kaya, Ruya; Taslimi, Parham; Demir, Yeliz
    In this work, the synthesis, crystal structure, characterization, and enzyme inhibition effects of the novel a series of 2-aminopyridine liganded Pd(II) N-heterocyclic carbene (NHC) complexes were examined. These complexes of the Pd-based were synthesized from PEPPSI complexes and 2-aminopyridine. The novel complexes were characterized by using C-13 NMR, H-1 NMR, elemental analysis, and FTIR spectroscopy techniques. Also, crystal structures of the two compounds were recorded by using single-crystal X-ray diffraction assay. Also, these complexes were tested toward some metabolic enzymes like a-glycosidase, aldose reductase, butyrylcholinesterase, acetylcholinesterase enzymes, and carbonic anhydrase I, and II isoforms. The novel 2-aminopyridine liganded (NHC) PdI2(2-aminopyridine) complexes (1a-i) showed Ki values of in range of 5.78 +/- 0.33-22.51 +/- 8.59 nM against hCA I, 13.77 +/- 2.21-30.81 +/- 4.87 nM against hCA II, 0.44 +/- 0.08-1.87 +/- 0.11 nM against AChE and 3.25 +/- 0.34-12.89 +/- 4.77 nM against BChE. Additionally, we studied the inhibition effect of these derivatives on aldose reductase and alpha-glycosidase enzymes. For these compounds, compound 1d showed maximum inhibition effect against AR with a Ki value of 360.37 +/- 55.82 nM. Finally, all compounds were tested for the inhibition of alpha-glycosidase enzyme, which recorded efficient inhibition profiles with Ki values in the range of 4.44 +/- 0.65-12.67 +/- 2.50 nM against aglycosidase.
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    Novel 2-methylimidazolium salts: Synthesis, characterization, molecular docking, and carbonic anhydrase and acetylcholinesterase inhibitory properties
    (Academic Press Inc Elsevier Science, 2020) Bal, Selma; Kaya, Ruya; Gok, Yetkin; Taslimi, Parham; Aktas, Aydin; Karaman, Muhammet; Gulcin, Ilhami
    In this work, structures of different imidazolium compounds were designed and synthesized. These compounds were synthesized from 2-methylimidazole and alkyl/aryl halides. Their structures were characterized by using H-1 NMR, C-13 NMR, FTIR spectroscopic techniques. All the synthesized compounds were tested for their inhibition activities on different enzymes. Inhibition experiments gave good and moderate results, proving their activities of these compounds as anticholinergics potential. These obtained novel 2-methylimidazolium salts (1a-e and 2a-e) molecules were effective inhibitors of the carbonic anhydrase I and II isozymes (hCA I and II) and acetylcholinesterase (AChE) enzymes with Ki values in the range of 26.45 +/- 6.49-77.60 +/- 9.53 nM for hCA I, 27.87 +/- 5.00-86.61 +/- 5.71 nM for hCA II, and 1.15 +/- 0.19-8.89 +/- 0.49 nM for AChE, respectively. AChE enzyme inhibitors are the most common drugs applied in the therapy of diseases such as senile dementia, Alzheimer's disease, ataxia, Parkinson's disease, and among others.
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    Novel morpholine liganded Pd-based N-heterocyclic carbene complexes: Synthesis, characterization, crystal structure, antidiabetic and anticholinergic properties
    (Pergamon-Elsevier Science Ltd, 2019) Aktas, Aydin; Celepci, Duygu Barut; Kaya, Ruya; Taslimi, Parham; Gok, Yetkin; Aygun, Muhittin; Gulcin, Ilhami
    This study involves the synthesis of novel N-heterocyclic carbene (NHC)PdX2(morpholine) complexes (1a-i). These Pd-based complexes are synthesized from pyridine enhanced precatalyst preparation stabilization and initiation (PEPPSI) complexes and morpholine. The new complexes were characterized by spectroscopy (IR, H-1 and C-13 NMR) techniques. Also, the crystal structures of lb and if were obtained by utilizing the single-crystal X-ray diffraction method. The synthesized compounds in this study were investigated for their inhibition action against equin serum butyrylcholinesterase (BChE) and Electrophorus electricus acetylcholinesterase (AChE) as the capability drug aims for Alzheimer's disease (AD). These novel morpholine liganded Pd-based N-heterocyclic complexes were good inhibitors of BChE, alpha-glycosidase, cytosolic carbonic anhydrase I and II isoforms (hCA I and II), and AChE, with K-i values in the range of 10.77 +/- 1.01-45.86 +/- 5.65 mu M for hCA I, 25.42 +/- 5.18-57.82 +/- 3.01 mu M for hCA II, 12.26 +/- 3.32-50.36 +/- 6.19 mu M for a-glycosidase, 9.97 +/- 1.26-60.75 +/- 15.98 M for BChE, and 10.28 1.55-30.12 3.22 M for AChE. The inhibition of the alpha-glycosidase enzyme, an important carbohydrate hydrolyzing catalyst, could be used as one of the efficient methodologies in both treating and preventing diabetes by controlling the suppressing postprandial hyperglycemia and postprandial glucose amounts. (C) 2018 Elsevier Ltd. All rights reserved.
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    Novel silver(I)N-heterocyclic carbene complexes bearing 2-(4-hydroxyphenyl)ethyl group: Synthesis, characterization, and enzyme inhibition properties
    (Wiley, 2021) Behcet, Ayten; Aktas, Aydin; Gok, Yetkin; Kaya, Ruya; Taslimi, Parham; Gulcin, Ilhami
    Herein, novel silver-based N-heterocyclic carbene (NHC) complexes bearing 2-(4-hydroxyphenyl)ethyl group were synthesized. Novel Ag(I)NHC complexes were synthesized from the 2-(4-hydroxyphenyl)ethyl-substituted benzimidazolium salts and silver oxide via in situ deprotonation method. The successful formation of all Ag(I)NHC complexes was proved by using H-1 NMR, C-13 NMR, FTIR spectroscopy, and elemental analysis techniques. In addition, their inhibitory effects have been investigated of these substances on acetylcholinesterase (AChE), alpha-glycosidase (alpha-Gly), human carbonic anhydrase I (hCA I), and human carbonic anhydrase II (hCA II) enzymes. It has been seen that all compounds have a better ability to inhibit compared with existing tried inhibitors. Among these, the best inhibitor against AChE enzyme is 1g (K-i : 9.54 +/- 0.98 mu M and IC50 : 17.40), and against alpha-Gly, 1c showed the highest effect (K-i 3.09 +/- 0.36 mu M and IC50 7.91). The best inhibitor against hCA I and hCA II enzymes are 1c and 1g compounds. For hCA I and hCA II, IC50 values were calculated as 17.85 and 9.06 mu M and K-i values were measured as 5.45 +/- 2.02 and 8.99 +/- 2.02 mu M, respectively.
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    Synthesis, characterization and bioactivities of dative donor ligand N-heterocyclic carbene (NHC) precursors and their Ag(I)NHC coordination compounds
    (Pergamon-Elsevier Science Ltd, 2021) Kazanci, Ali; Gok, Yetkin; Kaya, Ruya; Aktas, Aydin; Taslimi, Parham; Gulcin, Ilhami
    This study contains the synthesis of N-phthalimidomethyl-substituted NHC precursors and their Ag(I) NHC coordination compounds. The NHC precursors were synthesized from the 1-(N-phthalimidomethyl)benzimidazole and alkyl/aryl halide. The Ag(I)NHC coordination compounds were synthesized from the N-phthalimidomethyl substituted benzimidazolium salts and silver oxide via the in-situ deprotonation method. The formation of all compounds was proved fully by H-1 NMR, C-13 NMR, FTIR and elemental analysis techniques. Also, these novel N-phthalimidomethyl substituted NHC precursors and Ag(I) NHC coordination compounds were found as effective inhibitors for acetylcholinesterase (AChE), human carbonic anhydrase I isoenzyme (hCA I), human carbonic anhydrase II isoenzyme (hCA II), and butyrylcholinesterase (BChE) with inhibition constants (K(i)s) in the range of 1.00 +/- 0.14-2.31 +/- 0.58 mu M for hCA I, 1.30 +/- 0.21-2.85 +/- 0.56 mu M for hCA II, 0.35 +/- 0.06-2.58 +/- 0.70 mu M for AChE, and 0.42 +/- 0.01- 1.27 +/- 0.16 mu M for BChE, respectively. (C) 2020 Elsevier Ltd. All rights reserved.