Synthesis of nitrogen, phosphorus, selenium and sulfur-containing heterocyclic compounds – Determination of their carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase and α-glycosidase inhibition properties

Gülçın, İlhami; Трофимов, Б. А.; Kaya, Rüya; Taslimi, Parham; Собенина, Л. Н.; Schmidt, Elena Yu.; Петрова, О. В.; Малышева, С. Ф.; Гусарова, Н. К.; Farzaliyev, Vagif; Sujayev, Afsun; Alwasel, Saleh; Supuran, Claudiu T.

doi:10.1016/j.bioorg.2020.104171

Cited by 81 publications

(30 citation statements)

References 111 publications

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“…The measurements were spectrophotometrically recorded at 348 nm. [ 55–57 ] However, the inhibitory effects of AChE from electric eel ( Electrophorus electricus ) and BChE from equine serum were determined according to the method of Ellman et al [ 58 ] They were recorded spectrophotometrically at 412 nm using acetylthiocholine iodide and butyrylcholine iodide, and recorded as enzymatic reaction substrates according to previous studies. 5,5ʹ‐Dithio‐bis(2‐nitro‐benzoic acid) was used as a substrate to measure AChE activity.…”

Section: Methodsmentioning

confidence: 99%

New quinoxalin‐1,3,4‐oxadiazole derivatives: Synthesis, characterization, in vitro biological evaluations, and molecular modeling studies

Mirzazadeh

Asgari

Barzegari

et al. 2021

Archiv der Pharmazie

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A new series of quinoxalin‐1,3,4‐oxadiazole (10a–l) derivatives was synthesized and evaluated against some metabolic enzymes including human carbonic anhydrase (hCA) isoenzymes I and II (carbonic anhydrases I and II), cholinesterase (acetylcholinesterase and butyrylcholinesterase), and α‐glucosidase. Obtained data revealed that all the synthesized compounds were more potent as compared with the used standard inhibitors against studied target enzymes. Among the synthesized compounds, 4‐fluoro derivative (10f) against hCA I, 4‐chloro derivative (10i) against hCA II, 3‐fluoro derivative (10e) against acetylcholinesterase and butyrylcholinesterase, and 3‐bromo derivative (10k) against α‐glucosidase were the most potent compounds with inhibitory activity around 1.8‐ to 7.37‐fold better than standard inhibitors. Furthermore, docking studies of these compounds were performed at the active site of their target enzymes.

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Section: Methodsmentioning

confidence: 99%

New quinoxalin‐1,3,4‐oxadiazole derivatives: Synthesis, characterization, in vitro biological evaluations, and molecular modeling studies

Mirzazadeh

Asgari

Barzegari

et al. 2021

Archiv der Pharmazie

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“…Among the diverse reasons that were mentioned for pathogenesis of AD, reduce of acetylcholine (ACh) as main neurotransmitter in brain, formation of neurofibrillary tangles and amyloid β‐peptide (Aβ) plaques in the brain, and oxidative stress seem more significant than the others. [ 44,45 ] Today, the main drugs to treat AD are acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitors. [ 46,47 ]…”

Section: Introductionmentioning

confidence: 99%

Silver N‐heterocyclic carbene complexes bearing fluorinated benzyl group: Synthesis, characterization, crystal structure, computational studies, and inhibitory properties against some metabolic enzymes

Bal

Demirci

Şen

et al. 2021

Applied Organom Chemis

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A series of the silver N‐heterocyclic carbene (NHC) complexes have been synthesized from the reactions between benzimidazolium salts bearing fluorinated benzyl group and Ag2O via the deprotonation method. All Ag(I)NHC complexes were characterized by known spectroscopic techniques (1H nuclear magnetic resonance [NMR], 13C NMR, and Fourier transform infrared [FT‐IR]) and elemental analysis. The molecular structures of the two complexes were unambiguously elucidated through single‐crystal X‐ray diffraction analysis. Namely, X‐ray studies show that the coordination geometry around the Ag(I) atom in the case of complex 2c is revealed to be almost linear with C–Ag–Cl angle, whereas in complex 2e, it appears as a nonlinear structure. The inhibitory profiles of these new complexes are investigated on some metabolic enzymes. Representatively, the most potent complex against human carbonic anhydrase isoenzymes I and II (hCAs I and II), 2d, was 1.8 times more potent than standard inhibitor acetazolamide against hCAs I and II. On the other hand, complexes 2c and 2b as most potent compounds against both cholinesterase enzymes was around 5 and 1.6 times more potent than tacrine against acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), respectively. The most active α‐glucosidase inhibitor 2d had similar activity to acarbose as a standard inhibitor. Furthermore, it confirms its in vitro studies as a result of molecular docking studies for each enzyme with (i) binding energy and inhibition constant values and (ii) the definition of the best conformation and nonbonding interactions of the related complexes (2b, 2c, and 2d) against the different target proteins.

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“…The CA catalyzes the reversible hydration of CO 2 to HCO 3 − ions and appears in mammal tissues generally. There is only an active zinc atom for catalyze in its active district [32] . Zinc is the cofactor of many enzymes which have important roles in growth, immunity, cell respiration, redox reactions, and protein synthesis [33] …”

Section: Introductionmentioning

confidence: 99%

“…There is only an active zinc atom for catalyze in its active district. [32] Zinc is the cofactor of many enzymes which have important roles in growth, immunity, cell respiration, redox reactions, and protein synthesis. [33] The CA enzyme is affected by the pathologic situation that occured in many parts of the organs and tissues of metabolism.…”

Section: Introductionmentioning

confidence: 99%

Inhibition Profiles of Some Symmetric Sulfamides Derived from Phenethylamines on Human Carbonic Anhydrase I, and II Isoenzymes

Topal

Aksu

Gülçın

et al. 2021

Chemistry & Biodiversity

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In this work, the inhibitory effect of some symmetric sulfamides derived from phenethylamines were determined against human carbonic anhydrase (hCA) I, and II isoenzymes, and compared with standard compound acetazolamide. IC50 values were obtained from the Enzyme activity (%)‐[Symmetric sulfamides] graphs. Also, Ki values were calculated from the Lineweaver‐Burk graphs. Some symmetric sulfamides compounds (11–18) demonstrated excellent inhibition effects against hCA I, and II isoenzymes. These compounds demonstrated effective inhibitory profiles with IC50 values in ranging from 21.66–28.88 nM against hCA I, 14.44–30.13 nM against hCA II. Among these compounds, the best Ki value for hCA I (Ki: 8.34±1.60 nM) and hCA II (Ki: 16.40±1.00 nM) is compound number 11. Besides, the IC50 value of acetazolamide used as a standard was determined as hCA I, hCA II 57.75 nM, 49.50 nM, respectively. Moreover, in silico ADME‐Tox study showed that all synthesized compounds (11–18) had good oral bioavailability in light of Jorgensen's rule of three, and of Lipinski's rule of five.

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Synthesis of nitrogen, phosphorus, selenium and sulfur-containing heterocyclic compounds – Determination of their carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase and α-glycosidase inhibition properties

Cited by 81 publications

References 111 publications

New quinoxalin‐1,3,4‐oxadiazole derivatives: Synthesis, characterization, in vitro biological evaluations, and molecular modeling studies

New quinoxalin‐1,3,4‐oxadiazole derivatives: Synthesis, characterization, in vitro biological evaluations, and molecular modeling studies

Silver N‐heterocyclic carbene complexes bearing fluorinated benzyl group: Synthesis, characterization, crystal structure, computational studies, and inhibitory properties against some metabolic enzymes

Inhibition Profiles of Some Symmetric Sulfamides Derived from Phenethylamines on Human Carbonic Anhydrase I, and II Isoenzymes

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