The effects of some avermectins on bovine carbonic anhydrase enzyme

Köse, Leyla Polat; Gülçın, İlhami; Özdemir, Haşan; Atasever, Ali; Alwasel, Saleh; Supuran, Claudiu T.

doi:10.3109/14756366.2015.1064406

Cited by 52 publications

(28 citation statements)

References 79 publications

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“…Also, the utilization and development of new effective AChEIs is highly desired. Currently the most prescribed AChEIs are Tacrine, Galantamine, Rivastigmine, and Donepezil [55]. In the present study, AChE was very effectively inhibited by β-lactam derivatives 1 – 11 , with K i value in the range of 0.25 ± 0.019–1.13 ± 0.472 nM (Table 2) and calculated from Lineweaver-Burk plots [56].…”

Section: Resultssupporting

confidence: 51%

Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan β-Lactam Derivatives

Genc

Kalın

Köksal

et al. 2016

IJMS

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β-Lactams are pharmacologically important compounds because of their various biological uses, including antibiotic and so on. β-Lactams were synthesized from benzylidene-inden derivatives and acetoxyacetyl chloride. The inhibitory effect of these compounds was examined for human carbonic anhydrase I and II (hCA I, and II) and acetylcholinesterase (AChE). The results reveal that β-lactams are inhibitors of hCA I, II and AChE. The Ki values of β-lactams (2a–k) were 0.44–6.29 nM against hCA I, 0.93–8.34 nM against hCA II, and 0.25–1.13 nM against AChE. Our findings indicate that β-lactams (2a–k) inhibit both carbonic anhydrases (CA) isoenzymes and AChE at low nanomolar concentrations.

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Section: Resultssupporting

confidence: 51%

Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan β-Lactam Derivatives

Genc

Kalın

Köksal

et al. 2016

IJMS

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“…Voriconazole is an antifungal medication used to treat a number of fungal infections, and its inhibitory effects against some metabolic enzymes are shown in Table and Figures . Previous research has clearly indicated that the inhibitory effect of Voriconazole against hCA I, hCA II, AChE, and α‐glycosidase is greater than or equal to that of morphine, antioxidant phenols, hydroquinone, taxifolin, spirobisnaphthalenes, caffeic acid phenethyl ester, rosmarinic acid, some hydroperoxides, alcohols and acetates, some ureas, eugenol derivatives, lignans, thioureas, flavonoids, synephrine and phenylephrine, avermectins, antibiotics, and TAC derivatives . The present study adds to this previous literature (Table ).…”

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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“…Moreover, they have differences in tissue location and distribution; cytosolic (CA I–III, VII, and XIII), membrane bound (CA IV, IX, XII, XIV, XV), two mitochondrial (CA VA and VB), and one secreted (CA VI) in human saliva and serum. Also, there are three uncatalytic isoenzymes (CA VIII, X, and XI), which their functions are not yet fully understood .…”

Section: Introductionmentioning

confidence: 99%

Novel NHC Precursors: Synthesis, Characterization, and Carbonic Anhydrase and Acetylcholinesterase Inhibitory Properties

Aktaş

Taslimi

Gülçın

et al. 2017

Archiv der Pharmazie

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Three series of imidazolidinium ligands (NHC precursors) substituted with 4-vinylbenzyl, 2-methyl-1,4-benzodioxane, and N-propylphthalimide were synthesized. N-Heterocyclic carbene (NHC) precursors were prepared from N-alkylimidazoline and alkyl halides. The novel NHC precursors were characterized by H NMR, C NMR, FTIR spectroscopy, and elemental analysis techniques. The enzymes inhibition activities of the NHC precursors were investigated against the cytosolic human carbonic anhydrase I and II isoenzymes (hCA I and II) and the acetylcholinesterase (AChE) enzyme. The inhibition parameters (IC and K values) were calculated by spectrophotometric method. The inhibition constants (K ) were found to be in the range of 166.65-635.38 nM for hCA I, 78.79-246.17 nM for hCA II, and 23.42-62.04 nM for AChE. Also, the inhibitory effects of the novel synthesized NHCs were compared to acetazolamide as a clinical CA isoenzymes inhibitor and tacrine as a clinical cholinergic enzymes inhibitor.

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The effects of some avermectins on bovine carbonic anhydrase enzyme

Cited by 52 publications

References 79 publications

Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan β-Lactam Derivatives

Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan β-Lactam Derivatives

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

Novel NHC Precursors: Synthesis, Characterization, and Carbonic Anhydrase and Acetylcholinesterase Inhibitory Properties

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