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Acetylphenyl-substituted imidazolium salts: synthesis, characterization, in silico studies and inhibitory properties against some metabolic enzymes
(Springer, 2023) Demirci, Ozlem; Tezcan, Burcu; Demir, Yeliz; Taskin-Tok, Tugba; Gok, Yetkin; Aktas, Aydin; Guzel, Bilgehan
Herein, we present how to synthesize thirteen new 1-(4-acetylphenyl)-3-alkylimidazolium salts by reacting 4-(1-H-imidazol-1-yl)acetophenone with a variety of benzyl halides that contain either electron-donating or electron-withdrawing groups. The structures of the new imidazolium salts were conformed using different spectroscopic methods (H-1 NMR, C-13 NMR, F-19 NMR, and FTIR) and elemental analysis techniques. Furthermore, these compounds' the carbonic anhydrase (hCAs) and acetylcholinesterase (AChE) enzyme inhibition activities were investigated. They showed a highly potent inhibition effect toward AChE and hCAs with K-i values in the range of 8.30 & PLUSMN; 1.71 to 120.77 & PLUSMN; 8.61 nM for AChE, 16.97 & PLUSMN; 2.04 to 84.45 & PLUSMN; 13.78 nM for hCA I, and 14.09 & PLUSMN; 2.99 to 69.33 & PLUSMN; 17.35 nM for hCA II, respectively. Most of the synthesized imidazolium salts appeared to be more potent than the standard inhibitor of tacrine (TAC) against AChE and Acetazolamide (AZA) against CA. In the meantime, to prospect for potential synthesized imidazolium salt inhibitor(s) against AChE and hCAs, molecular docking and an ADMET-based approach were exerted.
Benzimidazolium Salts Bearing Nitrile Moieties: Synthesis, Enzyme Inhibition Profiling, and Molecular Docking Analysis for Carbonic Anhydrase and Acetylcholinesterase
(Wiley-V C H Verlag Gmbh, 2023) Oner, Erkan; Gok, Yetkin; Demir, Yeliz; Taskin-Tok, Tugba; Aktas, Aydin; Gulcin, Ilhami; Yalin, Serap
This report presents the synthesis and characterization of a range of benzimidazolium salts featuring 3-cyanopropyl groups on the 1st nitrogen atom and varied alkyl groups on the 3rd nitrogen atom within the benzimidazole structure. Benzimidazolium salts were synthesized by N-alkylation of 1-alkyl benzimidazole with 3-cyanopropyl-bromide. The new salts were characterized by 1H and 13C-NMR, FT-IR spectroscopic and elemental analysis techniques. In this study, the enzyme inhibition abilities of seven nitrile substituted benzimidazolium salts were investigated against acetylcholinesterase (AChE) and carbonic anhydrase isoenzymes I and II (hCA I and hCA II). They showed a highly potent inhibition effect on AChE, hCA I and hCA II (Ki values are in the range of 26.71-119.09 nM for AChE, 19.77 to 133.68 nM for hCA I and 13.09 to 266.38 nM for hCA II). Reflecting the binding mode of the synthesized cyanopropyl series, the importance of the 2,3,5,6-tetramethylbenzyl, 3-methylbenzyl and 3-benzyl groups for optimal interactions with target proteins, evaluated by molecular docking studies. At the same time, the docking findings support the inhibition constants (Ki) values of the related compounds in this study. Potential compounds were also evaluated by their pharmacokinetic properties were predicted. image
Benzimidazolium Salts Containing Trifluoromethoxybenzyl: Synthesis, Characterization, Crystal Structure, Molecular Docking Studies and Enzymes Inhibitory Properties
(Wiley-V C H Verlag Gmbh, 2022) Hamide, Mahmut; Gok, Yetkin; Demir, Yeliz; Sevincek, Resul; Taskin-Tok, Tugba; Tezcan, Burcu; Aktas, Aydin
The method for producing 4-trifluoromethoxybenzyl substituted benzimidazolium salts is described in this article. The method is based on the reaction of 4-trifluoromethoxybenzyl substituent alkylating agent with 1-alkylbenzimidazole. This method yielded 1-(4-trifluoromethoxybenzyl)-3-alkylbenzimidazolium bromide salts. These benzimidazolium salts were characterized by using H-1-NMR, C-13-NMR, FT-IR spectroscopy, and elemental analysis techniques. The crystal structure of 1f was enlightened by single crystal X-ray diffraction studies. Also, the enzyme inhibition effects of the synthesised compounds were investigated. They demonstrated highly potent inhibition effect on acetylcholinesterase (AChE) and carbonic anhydrases (hCAs) (K-i values are in the range of 7.24 +/- 0.99 to 39.12 +/- 5.66 nM, 5.57 +/- 0.96 to 43.07 +/- 11.76 nM, and 4.38 +/- 0.43 to 18.68 +/- 3.60 nM for AChE, hCA I, and hCA II, respectively). In molecular docking study, the interactions of active compounds showing activity against AChE and hCAs enzymes were examined. The most active compound 1f has -10.90 kcal/mol binding energy value against AChE enzyme, and the potential structure compound 1e, which has activity against hCA I and hCA II enzymes, was -7.51 and -8.93 kcal/mol, respectively.
Bisbenzimidazole salts and their in silico-in vitro inhibitory abilities on hCA I, hCA II, and AChE enzymes
(Springer Wien, 2024) Yilmaz, Ulku; Demir, Yeliz; Tok, Tugba Taskin; Gok, Yetkin; Aktas, Aydin; Gulcin, Ilhami
Eight new bisbenzimidazolium halides were prepared from alkyl halides and 4,4 '-bis[(benzimidazol-1-yl)methyl]-1,1 '-biphenyl.The structures of the benzimidazole salts were characterized using elemental analysis techniques as well as 1H, 13C NMR, and FT-IR spectroscopic methods. The inhibitory effects of the benzimidazole derivatives were measured against human carbonic anhydrase I (hCA I), human carbonic anhydrase II (hCA II), and acetylcholinesterase (AChE) enzymes. All benzimidazolium halides exhibited significant enzyme inhibitory properties. They showed highly potent inhibitory effect on AChE and hCAs (Ki values are in the range of 15.7 +/- 0.8 to 49.7 +/- 10.1 nM, 14.6 +/- 1.5 to 70.7 +/- 2.7 nM, and 17.4 +/- 2.8 to 38 +/- 10 nM for AChE, hCA I, and hCA II, respectively). The binding orientation of the synthesized bisbenzimidazolium halides was evaluated by molecular docking studies, reflecting the importance of the p-methylbenzyl, m-methylbenzyl, p-nitrophenethyl, and 3-(1,3-dioxoisoindolin-2-yl)methyl) groups in protein-ligand interaction. The docking results support the Ki values of the respective compounds in this study. The structure-activity relationships against the various targets are clearly shown in three dimensions at the atomic level by their interactions with the mentioned enzymes.
Fluorinated benzimidazolium salts: Synthesis, characterization, molecular docking studies and inhibitory properties against some metabolic enzymes
(Elsevier Science Sa, 2023) Zengin, Ramazan; Gok, Yetkin; Demir, Yeliz; Sen, Betul; Taskin-Tok, Tugba; Aktas, Aydin; Demirci, Ozlem
Here, a number of symmetric and unsymmetric N-heterocyclic carbene (NHC) precursors based on benzimidazol-2-ylidene are synthesized. The N-benzyl substituent in these compounds has an electron-withdrawing group (F) at the para position. The structure of these compounds was characterized using elemental analysis and various spectroscopic methods (FTIR and NMR). The molecular and crystal structures of compound 1f and compound 1h were unambiguously elucidated through single-crystal X-ray diffraction analysis. According to the X-ray studies, compound 1f exhibits the formation of a U-shaped molecule whereas compound 1h has a Z-shape formation. In addition, the enzyme inhibition activities of these compounds were investigated against acetylcholinesterase (AChE) and carbonic anhydrases (hCAs). They showed a highly potent inhibition effect on AChE and hCAs (Ki values are in the range of 14.84 +/- 1.91 to 174.80 +/- 23.60 nM for AChE, 22.41 +/- 1.93 to 188.67 +/- 27.05 nM for hCA I and 35.29 +/- 7.21 to 136.55 +/- 17.61 nM for hCA II). These results may contribute to the design and development of new drug candidates, particularly for treatment of some widespread disorders displayed in the world including Alzheimer's disease and glaucoma.
Investigation of Some Metabolic Enzyme Inhibition Properties of Novel Chalcone-Cu Complexes
(Wiley-V C H Verlag Gmbh, 2024) Ebiri, Rustem; Turgut, Muhammet; Anil, Derya Aktas; Demir, Yeliz; Saglamtas, Ruya; Alagoz, M. Abdullah; Algul, Oztekin
Fourteen novel Chalcone-Cu complexes were effectively synthesized in this work. The newly synthesized Chalcone-Cu complexes were assessed for their effects on human carbonic anhydrase isoenzymes I and II, acetylcholinesterase enzymes, and antioxidant activity. The intricate compounds exhibited Ki values ranging from 41.65-190.42 nM against hCA I, 15.79-259.07 nM against hCA II, and 14.36-175.73 nM against AChE enzymes. These complexes demonstrated potent inhibitory profiles against the specified metabolic enzymes, surpassing the inhibitory effects of acetazolamide (for hCA I and II) and tacrine (for AChE). The antioxidant properties of the compounds were assessed using DPPH and ABTS radical scavenging assays, revealing that the complexes had moderate to high efficacy in neutralizing free radicals. All complexes underwent molecular docking experiments. Compounds 14, 22, and 23 yielded the highest docking scores. Compound 14 demonstrated a docking score of -6.414 kcal/mol against hCAI, whereas compound 23 attained a docking score of -6.697 kcal/mol against hCA II. Compound 22 exhibited the most favorable docking score of -9.645 kcal/mol against AChE. The acquired results have the potential to help towards the development of new drugs containing Cu complex structures for the treatment of prevalent ailments such as glaucoma and Alzheimer's diseases. This study unveils the potential of Chalcone-Cu complexes as potent enzyme inhibitors (hCA I and II and AChE) with antioxidant properties. The structural insights, inhibitory profiles, and molecular docking results underscore their therapeutic potential for neurological disorders. The findings present a foundation for further exploration and drug development in the realm of Chalcone-Cu compounds. image
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.
Organohalogen chalcones: design, synthesis, ADMET prediction, molecular dynamics study and inhibition effect on acetylcholinesterase and carbonic anhydrase
(Springer, 2024) Aydin, Busra Ozturk; Anil, Derya Aktas; Demir, Yeliz; Alagoz, Mehmet Abdullah
In an effort to discover potential acetylcholinesterase (AChE) and carbonic anhydrase (CA) inhibitors, a novel series of organohalogen chalcone derivatives (12-20, 23-30) was synthesized, and their chemical structures were characterized by spectral analysis. They showed a highly potent inhibition effect on AChE and hCAs (Ki values range from 5.07 +/- 0.062 to 65.53 +/- 4.36 nM for AChE, 13.54 +/- 2.55 to 94.11 +/- 10.39 nM for hCA I, and 5.21 +/- 0.54 to 57.44 +/- 3.12 nM for hCA II). In addition, the chalcone derivatives with the highest inhibitor score docked into the active site of the indicated metabolic enzyme receptors, and their absorption, metabolism, and toxic properties were evaluated according to ADMET's estimation.Compounds 16 and 19 exhibited the highest inhibition score, emerged as lead compounds, and inspired the development of more potent compounds.
The palladium-based complexes bearing 1,3-dibenzylbenzimidazolium with morpholine, triphenylphosphine, and pyridine derivate ligands: synthesis, characterization, structure and enzyme inhibitions
(Cell Press, 2022) Aktas, Aydin; Yakali, Gul; Demir, Yeliz; Gulcin, Ilhami; Aygun, Muhittin; Gok, Yetkin
The palladium-based complexes bearing N-heterocyclic carbene (NHC) ligand have long attracted attention as active catalysts for many catalytic reactions. Recently, the biological activities of these complexes, which are stable to air and moisture, have also been wondered. With the aim, we report the synthesis of a series of (NHC) Pd(Br2)(L) complexes (NHC: 1,3-dibenzylbenzimidazolium, L: morpholine, triphenylphosphine, pyridine, 3-chloropyridine, and 2-aminopyridine). All complexes were characterized by NMR (1H and 13C), FTIR spectroscopic and elemental analysis techniques. In addition, the single crystal structures of the complex 3, 4, and 6 were determined through single crystal x-ray crystallographic method. Furthermore, the carbonic anhydrase I and II isoenzymes (hCAs) and acetylcholinesterase (AChE) inhibition effects of these palladium-based complexes bearing NHC ligand were investigated. They showed highly potent inhibition effect with Ki values are between 10.06 +/- 1.49-68.56 +/- 11.53 nM for hCA I isoenzyme, 7.74 +/- 0.66 to 49.39 +/- 6.50 nM for hCA II isoenzyme and 22.83 +/- 3.21 to 64.09 +/- 9.05 nM for AChE enzyme.
Pentafluorobenzyl-substituted benzimidazolium salts: Synthesis, characterization, crystal structures, computational studies and inhibitory properties of some metabolic enzymes
(Elsevier, 2022) Hamide, Mahmut; Gok, Yetkin; Demir, Yeliz; Yakali, Gul; Tok, Tugba Taskin; Aktas, Aydin; Sevincek, Resul
This work contains the synthesis and characterization of the pentafluorobenzyl-substituted benzimidazolium salts which N -heterocyclic carbene (NHC) precursors. All compounds were characterized by using 1 H, 13 C, and 19 F NMR, FT-IR spectroscopy, and elemental analysis techniques. All the spectroscopy and elemental analysis data fully confirm the proposed formulas. In the synthesized compounds, the molecular structures of compounds 1-(2-methylbenzyl)-3-(2,3,4,5,6-pentafluorobenzyl)benzimidazolium bromide ( 1b ), 1-(4-methylbenzyl)-3-(2,3,4,5,6-pentafluorobenzyl)benzimidazolium bromide ( 1d ) and 1-(4-trifluoromethylbenzyl)-3-(2,3,4,5,6-pentafluorobenzyl)benzimidazolium bromide ( 1f ) were enlightened by single crystal X-ray diffraction studies. After enzyme inhibition study, a new series of pentafluorobenzyl-substituted NHC precursors were determined to be highly potent inhibitors for acetylcholinesterase (AChE) enzyme and carbonic anhydrases (hCAs) isoenzymes. K i values were found in the range of 7.20 +/- 1.31 to 28.26 +/- 5.72 nM for AChE , 10.25 +/- 0.93 to 40.93 +/- 3.89 nM toward hCA I as pervasive metal containing enzymes present in prokaryotes and eukaryotes, and 3.33 +/- 0.15 to 58.22 +/- 6.99 nM for hCA II as the key enzyme promising strategy for the treatment of neurological disorders such as Alzheimer's disease. The molecular docking study performed for compounds had higher potential inhibitory properties involved in a novel series of pentafluorobenzyl-substituted NHC precursors based on the binding energy and interaction types against AChE and hCAs. (c) 2022 Elsevier B.V. All rights reserved.
Phthalimide-tethered imidazolium salts: Synthesis, characterization, enzyme inhibitory properties, and in silico studies
(Wiley-V C H Verlag Gmbh, 2022) Yigit, Murat; Demir, Yeliz; Celepci, Duygu Barut; Taskin-Tok, Tugba; Arinc, Ali; Yigit, Beyhan; Aygun, Muhittin
A series of new imidazolium salts were prepared in good yield by the reaction between 1-alkylimidazole and a variety of alkyl halides. The structures of the compounds were identified by FT-IR, H-1 NMR, and C-13 NMR spectroscopy, elemental analysis, and mass spectrometry. The crystal structure of 1b was determined by the single-crystal X-ray diffraction method. The phthalimide-tethered imidazolium salts exhibited inhibition abilities toward acetylcholinesterase (AChE) and human carbonic anhydrases (hCAs) I and II, with K-i values in the range of 24.63 +/- 3.45 to 305.51 +/- 35.98 nM for AChE, 33.56 +/- 3.71 to 218.01 +/- 25.21 nM for hCA I and 17.75 +/- 0.96 to 308.67 +/- 13.73 nM for hCA II. The results showed that the new imidazolium salts can play a key role in the treatment of Alzheimer's disease, epilepsy, glaucoma, and leukemia, which is related to their inhibition abilities of hCA I, hCA II, and AChE. Molecular docking and in silico absorption, distribution, metabolism, excretion and toxicity studies were used to look into how the imidazolium salts interacted with the specific protein targets. To better visualize and understand the binding positions and the influence of the imidazolium salts on hCA I, hCA II, and AChE conformations, each one was subjected to molecular docking simulations.
Structure-based inhibition of acetylcholinesterase and butyrylcholinesterase with 2-Aryl-6-carboxamide benzoxazole derivatives: synthesis, enzymatic assay, and in silico studies
(Springer, 2024) Kuzu, Burak; Alagoz, M. Abdullah; Demir, Yeliz; Gulcin, Ilhami; Burmaoglu, Serdar; Algul, Oztekin
An important research topic is the discovery of multifunctional compounds targeting different disease-causing components. This research aimed to design and synthesize a series of 2-aryl-6-carboxamide benzoxazole derivatives that inhibit cholinesterases on both the peripheral anionic and catalytic anionic sides. Compounds (7-48) were prepared from 4-amino-3-hydroxybenzoic acid in three steps. The Ellman test, molecular docking with Maestro, and molecular dynamics simulation studies with Desmond were done (Schrodinger, 12.8.117). Compound 36, the most potent compound among the 42 new compounds synthesized, had an inhibitory concentration of IC50 12.62 nM for AChE and IC50 25.45 nM for BChE (whereas donepezil was 69.3 nM and 63.0 nM, respectively). Additionally, compound 36 had docking values of - 7.29 kcal/mol for AChE and - 6.71 kcal/mol for BChE (whereas donepezil was - 6.49 kcal/mol and - 5.057 kcal/mol, respectively). Furthermore, molecular dynamics simulations revealed that compound 36 is stable in the active gorges of both AChE (average RMSD: 1.98 & Aring;) and BChE (average RMSD: 2.2 & Aring;) (donepezil had average RMSD: 1.65 & Aring; and 2.7 & Aring;, respectively). The results show that compound 36 is a potent, selective, mixed-type dual inhibitor of both acetylcholinesterase and butyrylcholinesterase. It does this by binding to both the catalytically active and peripheral anionic sites of cholinesterases at the same time. These findings show that target compounds may be useful for establishing the structural basis for new anti-Alzheimer agents. [GRAPHICS] .
SYNTHESIS AND ENZYME INHIBITORY PROPERTIES OF QUINOXALINE BRIDGED BIS(IMIDAZOLIUM) SALTS
(Pergamon-Elsevier Science Ltd, 2022) Yigit, Murat; Demir, Yeliz; Arinc, Ali; Yigit, Beyhan; Koca, Murat; Ozdemir, Ismail; Gulcin, Ilhami
In this study, a series of new salts containing quinoxaline and imidazole moieties were synthesized in good yield by the reaction of 2,3 -bis(bromomethyl)quinoxalines and 1-alkylimidazoles in N,N-dimethylformamide. These salts were characterized by elemental analysis, IR, H-1 NMR and C-13 NMR spectroscopy, which support the proposed structures. Furthermore, the enzyme inhibition activities of these compounds were investigated. They showed highly potent inhibition effect on acetylcholinesterase (AChE) and carbonic anhydrases (hCAs) (Ki values are in the range of 44.80 +/- 14.87 to 288.64 +/- 42.68 nM, 21.50 +/- 4.76 to 187.30 +/- 22.43 nM, and 5.81 +/- 0.71 to 164.52 +/- 26.0 nM for AChE, hCA I, and hCA II, respectively). Compound 3 showed the best inhibition effect for hCA I and compound 4 showed the best inhibition effect for hCA II and AChE.
Synthesis of 1,3-Disubtitituted Tetrahydropyrimidinium Salts and Determination of Their Biological Properties and Molecular Docking
(Wiley-V C H Verlag Gmbh, 2024) Karaca, Emine Ozge; Gurbuz, Nevin; Demir, Yeliz; Tuzun, Burak; Ozdemir, Ismail; Gulcin, Ilhami
Several of 3,4,5,6-tetrahydropyrimidinium salts with 1-methyl functionalization are produced. By using techniques for 1H-NMR, 13C-NMR, and IR spectroscopy, all compounds were investigated. Additionally, these compounds' abilities to block enzymes were looked into. They had a highly effective inhibitory effect on the isoenzymes of carbonic anhydrases I and II, butyrylcholinesterase (BChE), and acetylcholinesterase (AChE). Ki values were found in the range of 57.43 +/- 7.09-170.09 +/- 50.91 nM for AChE, 7.19 +/- 0.42-69.08 +/- 2.44 nM for BChE, and 46.48 +/- 5.74-203.38 +/- 46.15 nM for hCA I, and 30.19 +/- 4.03-171.96 +/- 30.27 nM for hCA II. As a result, 1,3-disubtitituted tetrahydroprimidinium salts exhibited potent inhibition profiles toward indicated metabolic enzymes. One of the most important methods for designing and creating novel, potent medications to treat Alzheimer's disease (AD) worldwide is the synthesis and discovery of new AChE and BChE inhibitors. The activities of synthesized 3,4,5,6-tetrahydropyrimidinium salts were compared against various proteins that are crystal structure of AChE (PDB ID: 4 M0E), crystal structure of BChE (PDB ID: 5NN0), crystal structure of hCA I (PDB ID: 2CAB), and crystal structure of hCA II (PDB ID: 3DC3), and then the drug properties of these molecules were examined. In this study, we have designed and synthesized a series of 1,3-disubtitituted tetrahydropyrimidinium salts were synthesized and characterized by IR and NMR spectra. These compounds were evaluated against the AChE, BChE, hCA I and hCA II enzymes. These compounds showed good enzyme inhibition profiles. The activities of the investigated 1,3-disubstituted tetrahydropyrimidinium salts were compared to the theoretical calculations results using molecular docking. image
Synthesis, characterisation, biological evaluation and in silico studies of sulphonamide Schiff bases
(Taylor & Francis Ltd, 2020) Durgun, Mustafa; Turkes, Cuneyt; Isik, Mesut; Demir, Yeliz; Sakli, Ali; Kuru, Ali; Guzel, Abdussamat
Sulphonamides are biologically important compounds with low toxicity, many bioactivities and cost-effectiveness. Eight sulphonamide derivatives were synthesised and characterised by FT-IR, C-13 NMR, H-1 NMR, LC-MS and elemental analysis. Their inhibitory effect on AChE, and carbonic anhydrase I and II enzyme activities was investigated. Their antioxidant activity was determined using different bioanalytical assays such as radical scavenging tests with ABTS(center dot+), and DPPH center dot+ as well as metal-reducing abilities with CUPRAC, and FRAP assays. All compounds showed satisfactory enzyme inhibitory potency in nanomolar concentrations against AChE and CA isoforms with K-I values ranging from 10.14 +/- 0.03 to 100.58 +/- 1.90 nM. Amine group containing derivatives showed high metal reduction activity and about 70% ABTS radical scavenging activity. Due to their antioxidant activity and AChE inhibition, these novel compounds may be considered as leads for investigations in neurodegenerative diseases.

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