Novel morpholine liganded Pd-based N-heterocyclic carbene complexes: Synthesis, characterization, crystal structure, antidiabetic and anticholinergic properties

Aktaş, Aydın; Celepci, Duygu Barut; Kaya, Rüya; Taslimi, Parham; Gök, Yetkın; Aygün, Muhıttın; Gülçın, İlhami

doi:10.1016/j.poly.2018.11.048

Cited by 71 publications

(40 citation statements)

References 74 publications

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“…For determination of CA activity, both esterase and hydratase activities have been commonly employed; however, esterase activity has been used more often because its substrate is more easily adjusted than hydratase. Esterase activity was used for determining inhibition type and K i values of inhibitors . In this paper, AZA was employed.…”

Section: Discussionmentioning

confidence: 99%

Inhibition profiles of Voriconazole against acetylcholinesterase, α‐glycosidase, and human carbonic anhydrase I and II isoenzymes

Topal

2019

J Biochem & Molecular Tox

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In this work, the inhibitory activity of Voriconazole was measured against some metabolic enzymes, including human carbonic anhydrase (hCA) I and II isoenzymes, acetylcholinesterase (AChE), and α‐glycosidase; the results were compared with standard compounds including acetazolamide, tacrine, and acarbose. Half maximal inhibition concentration (IC50) values were obtained from the enzyme activity (%)‐[Voriconazole] graphs, whereas Ki values were calculated from the Lineweaver‐Burk graphs. According to the results, the IC50 value of Voriconazole was 40.77 nM for α‐glycosidase, while the mean inhibition constant (Ki) value was 17.47 ± 1.51 nM for α‐glycosidase. The results make an important contribution to drug design and have pharmacological applications. In addition, the Voriconazole compound demonstrated excellent inhibitory effects against AChE and hCA isoforms I and II. Voriconazole had Ki values of 29.13 ± 3.57 nM against hCA I, 15.92 ± 1.90 nM against hCA II, and 10.50 ± 2.46 nM against AChE.

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Section: Discussionmentioning

confidence: 99%

Inhibition profiles of Voriconazole against acetylcholinesterase, α‐glycosidase, and human carbonic anhydrase I and II isoenzymes

Topal

2019

J Biochem & Molecular Tox

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“…[33][34][35] Unfortunately, this disease cannot be completely treated. [36,37] Uncontrolled blood sugar is the main problem of diabetes. [38,39] In Type-2 diabetes, either a decrease in insulin secretion in peripheral tissues or a disorder in insulin secretion is caused.…”

Section: Introductionmentioning

confidence: 99%

The inhibition profile of sesamol against α-glycosidase and acetylcholinesterase enzymes

Topal

2019

International Journal of Food Properties

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Sesamol (1,3-benzodioxol-5-ol) is found in the oilseed product, sesame. In our study, the inhibitory effects of sesamol compound on acetylcholinesterase and α-glycosidase enzymes were evaluated. Another aim of this study was to compare the inhibitory effects of sesamol to acarbose for α-glycosidase enzyme and tacrine for acetylcholinesterase (AChE). Sesamol exhibited noncompetitive inhibition for both metabolic enzymes. IC 50 values for AChE and αglycosidase enzymes were calculated as 86.63 nM and 99.00 nM, respectively. On the other hand, K i values were calculated as 46.68 nM and 75.33 nM for AChE and α-glycosidase enzymes, respectively. According to the obtained results showed effective inhibition at low concentrations. ARTICLE HISTORY

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“…Also, NHCs could form strong bonds with most transition metals thanks to their widely tunable structural and electronic properties . These beneficial properties have contributed to the recognition of NHCs as excellent nucleophilic organocatalysts in many fields of application, especially in material and medical sciences,, and also in organometallic chemistry thanks to synthesized homogeneous catalysis …”

Section: Introductionmentioning

confidence: 99%

2‐hydroxyethyl‐substituted (NHC)PdI₂(pyridine) (Pd‐PEPPSI) Complexes: Synthesis, Characterization and the Catalytic Activity in the Sonogashira Cross‐coupling Reaction

et al. 2019

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Here, new series of the 2‐hydroxyethyl‐substituted (NHC)PdI2(pyridine) (Pd‐PEPPSI) complexes have been synthesized. These complexes have been prepared from the 2‐hydroxyethyl‐substituted N‐heterocyclic carbene (NHC) precursors, palladium chloride and pyridine. The synthesized Pd‐PEPPSI complexes have been characterized by using 1H NMR, 13C NMR, FTIR spectroscopy and elemental analysis techniques. The catalytic activity of the 2‐hydroxyethyl‐substituted Pd‐PEPPSI complexes has been examined in the Sonogashira cross‐coupling reaction by using phenylacetylene and aryl bromide. The Pd‐PEPPSI complexes have demonstrated great activity in the Sonogashira cross‐coupling reaction. The molecular and crystal structures of the three of the Pd‐PEPPSI complexes were determined by single‐crystal X‐ray diffraction method. X‐ray studies show that all the molecular structures adopt slightly distorted square‐planar geometry around the palladium (II) center.

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Novel morpholine liganded Pd-based N-heterocyclic carbene complexes: Synthesis, characterization, crystal structure, antidiabetic and anticholinergic properties

Cited by 71 publications

References 74 publications

Inhibition profiles of Voriconazole against acetylcholinesterase, α‐glycosidase, and human carbonic anhydrase I and II isoenzymes

Inhibition profiles of Voriconazole against acetylcholinesterase, α‐glycosidase, and human carbonic anhydrase I and II isoenzymes

The inhibition profile of sesamol against α-glycosidase and acetylcholinesterase enzymes

2‐hydroxyethyl‐substituted (NHC)PdI₂(pyridine) (Pd‐PEPPSI) Complexes: Synthesis, Characterization and the Catalytic Activity in the Sonogashira Cross‐coupling Reaction

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Novel morpholine liganded Pd-based N-heterocyclic carbene complexes: Synthesis, characterization, crystal structure, antidiabetic and anticholinergic properties

Cited by 71 publications

References 74 publications

Inhibition profiles of Voriconazole against acetylcholinesterase, α‐glycosidase, and human carbonic anhydrase I and II isoenzymes

Inhibition profiles of Voriconazole against acetylcholinesterase, α‐glycosidase, and human carbonic anhydrase I and II isoenzymes

The inhibition profile of sesamol against α-glycosidase and acetylcholinesterase enzymes

2‐hydroxyethyl‐substituted (NHC)PdI2(pyridine) (Pd‐PEPPSI) Complexes: Synthesis, Characterization and the Catalytic Activity in the Sonogashira Cross‐coupling Reaction

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2‐hydroxyethyl‐substituted (NHC)PdI₂(pyridine) (Pd‐PEPPSI) Complexes: Synthesis, Characterization and the Catalytic Activity in the Sonogashira Cross‐coupling Reaction