RESUMO
In the article, various substituted derivatives of 1,2-aminopropanthiol (1a-g) have been prepared by a general and efficient method, in one-steps, starting from available thiirane and aromatic amines (aniline, o-toluidine) as a convenient source of sulfur and nitrogen. The synthesized compounds were fully characterized by spectral and analytical data. Seven novel compounds are synthesized. The biochemical properties indicating their potential for constituting an anti-Alzheimer's disease substance were also recorded revealing strong carbonic anhydrase I, and II, α-glycosidase, and acetylcholinesterase inhibitory effects. These synthesized novel 1,2-aminopropanthiols substituted derivatives (1a-g) were found to be effective inhibitors for the α-glycosidase, human carbonic anhydrase I and II, and acetylcholinesterase enzymes, with Ki values in the range of 11.47 ± 0.87-24.09 ± 6.37 µM for α-glycosidase, 29.30 ± 4.67-79.01 ± 4.49 µM for hCA I, 14.27 ± 2.82-30.85 ± 12.24 µM for hCA II and 5.76 ± 1.55-55.39 ± 2.27 µM for AChE, respectively. In the last step of this study, molecular docking calculations were obtained in order to compare the biological activities of indicated molecules against the enzymes of acetylcholinesterase, butyrylcholinesterase and α-glycosidase. Communicated by Ramaswamy H. Sarma.
Assuntos
Acetilcolinesterase , Anidrases Carbônicas , Acetilcolinesterase/metabolismo , Butirilcolinesterase , Inibidores da Colinesterase/farmacologia , Glicosídeo Hidrolases/metabolismo , Humanos , Simulação de Acoplamento Molecular , Estrutura Molecular , Relação Estrutura-AtividadeRESUMO
Cancer is a disease characterized by the continuous growth of cells without adherence to the rules that healthy normal cells obey. Carbonic anhydrase I and II (CA I and CA II) inhibitors are used for the treatment of some diseases. The available drugs in the market have limitations or side effects, which bring about the need to develop new drug candidate compound(s) to overcome the problems at issue. In this study, new pyrazole-sulphonamide hybrid compounds 4-[5-(1,3-benzodioxol-5-yl)-3-aryl-4,5-dihydro-1 H -pyrazol-1-yl]benzenesulphonamides (4a - 4j) were designed to discover new drug candidate compounds. The compounds 4a - 4j were synthesized and their chemical structures were confirmed using spectral techniques. The hypothesis tested was whether an introduction of methoxy and polymethoxy group(s) lead to an increased potency selectivity expression (PSE) value of the compound, which reflects cytotoxicity and selectivity of the compounds. The cytotoxicity of the compounds towards tumor cell lines were in the range of 6.7 - 400 µM. The compounds 4i (PSE2 = 461.5) and 4g (PSE1 = 193.2) had the highest PSE values in cytotoxicity assays. Ki values of the compounds were in the range of 59.8 ± 3.0 - 12.7 ± 1.7 nM towards hCA I and in the range of 24.1 ± 7.1 - 6.9 ± 1.5 nM towards hCA II. While the compounds 4b, 4f, 4g, and 4i showed promising cytotoxic effects, the compounds 4c and 4g had the inhibitory potency towards hCA I and hCA II, respectively. These compounds can be considered as lead compounds for further research.
RESUMO
In this study, we report the synthesis of novel tris-chalcones and testing of human carbonic anhydrase I, and II isoenzymes (hCA I, and hCA II), acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and α-glycosidase (α-Gly) inhibitors for the development of novel chalcone structures towards for treatment of some diseases. The compounds demonstrated Ki values between 13.6 ± 1.1 and 50.0 ± 17.1 nM on hCA I, 9.9 ± 0.8 and 39.5 ± 15.1 nM on hCA II, 3.1 ± 0.2 and 20.1 ± 1.9 nM on AChE, 4.9 ± 0.4 and 14.7 ± 5.2 nM on BChE and 3.9 ± 0.2 and 22.4 ± 10.7 nM on α-Gly enzymes. The results revealed that novel tris-chalcones can have promising drug potential for glaucoma, leukaemia, epilepsy; Alzheimer's disease that was associated with the high enzymatic activity of hCA I, hCA II, AChE, and BChE enzymes.
Assuntos
Acetilcolinesterase/química , Butirilcolinesterase/química , Inibidores da Anidrase Carbônica/farmacologia , Anidrases Carbônicas/química , Chalconas/síntese química , Chalconas/farmacologia , Inibidores da Colinesterase/farmacologia , Inibidores da Anidrase Carbônica/química , Inibidores da Colinesterase/química , HumanosRESUMO
Sulfur-containing pyrroles (1-3), tris(2-pyridyl)phosphine(selenide) sulfide (4-5) and 4-benzyl-6-(thiophen-2-yl)pyrimidin-2-amine (6) were synthesized and characterized by elemental analysis, IR and NMR spectra. In this study, the synthesized compounds of nitrogen, phosphorus, selenium and sulfur-containing heterocyclic compounds (1-6) were evaluated against the human erythrocyte carbonic anhydrase I, and II isoenzymes, acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and α-glycosidase enzymes. The synthesized heterocyclic compounds showed IC50 values in range of 33.32-60.79 nM against hCA I, and 37.05-66.64 nM against hCA II closely associated with various physiological and pathological processes. On the other hand, IC50 values were found in range of 13.13-22.21 nM against AChE, 0.54-31.22 nM against BChE, and 13.51-26.55 nM against α-glycosidase as a hydrolytic enzyme. As a result, nitrogen, phosphorus, selenium and sulfur-containing heterocyclic compounds (1-6) demonstrated potent inhibition profiles against indicated metabolic enzymes. Therefore, we believe that these results may contribute to the development of new drugs particularly in the treatment of some global disorders including glaucoma, Alzheimer's disease and diabetes.
Assuntos
Acetilcolinesterase/química , Butirilcolinesterase/química , Inibidores de Glicosídeo Hidrolases/química , Compostos Heterocíclicos/síntese química , Nitrogênio/química , Fósforo/química , Selênio/química , Compostos Heterocíclicos/química , Humanos , Relação Estrutura-AtividadeRESUMO
A series of compounds incorporating 3-(3-(2/3/4-substituted phenyl)triaz-1-en-1-yl) benzenesulfonamide moieties were synthesised and their chemical structure was confirmed by physico-chemical methods. Carbonic anhydrase (CA, EC 4.2.1.1) inhibitory effects of the compounds were evaluated against human isoforms hCA I and II. KI values of these sulphonamides were in the range of 21 ± 4-72 ± 2 nM towards hCA I and in the range of 16 ± 6-40 ± 2 nM against hCA II. The 4-fluoro substituted derivative might be considered as an interesting lead due to its effective inhibitory action against both hCA I and hCA II (KIs of 21 nM), a profile rarely seen among other sulphonamide CA inhibitors, making it of interest in systems where the activity of the two cytosolic isoforms is dysregulated.
Assuntos
Anidrase Carbônica II/antagonistas & inibidores , Anidrase Carbônica I/antagonistas & inibidores , Inibidores da Anidrase Carbônica/farmacologia , Sulfonamidas/farmacologia , Triazenos/farmacologia , Anidrase Carbônica I/metabolismo , Anidrase Carbônica II/metabolismo , Inibidores da Anidrase Carbônica/síntese química , Inibidores da Anidrase Carbônica/química , Relação Dose-Resposta a Droga , Humanos , Estrutura Molecular , Relação Estrutura-Atividade , Sulfonamidas/química , Triazenos/químicaRESUMO
The aim of this study was to investigate the effects of boric acid (BA) and borax (BX) on live weight and obesity associated molecules including leptin, L-carnitine, insulin-like growth factor 1 (IGF-I), and heat shock proteins 70 (HSP70) in rats fed with high-fat diet. A total of 60 rats were equally allocated as ND (normal diet), HF (high-fat diet), HF+BA, HF+BX, ND+BX, ND+BA. Body weight increases in HF+BA (85 g) and HF+BX (86 g) were significantly lower (p<0.05) compared to HF group (126 g). Boron treatment decreased serum L-carnitine level in high-fat diet (HF+BA 11.12 mg/L, HF+BX 10.51 mg/L, p<0.05) compared to HF group (15.57 mg/L), while no change was observed in groups ND+BA (7.55 mg/L) and ND+BX (7.57 mg/L) compared to group ND (8.29 mg/L). Neither BA nor BX supplementation in ND and HF groups altered the serum levels of HSP70 and leptin. BA and BX supplementation in rats fed HF resulted in a significant reduction in live weight. Boron compounds altered L-carnitine and IGF-1 levels in rats. These results indicate that boron compounds are beneficial in the treatment of obesity as well as in the prevention of high-fat diet-induced weight increase. Alterations in serum L-carnitine and IGF-1 levels in boron treated rats also indicate possible role of boron compounds in energy metabolism in response to high fat diet.
Assuntos
Boratos/química , Ácidos Bóricos/química , Carnitina , Fator de Crescimento Insulin-Like I , Animais , Carnitina/química , Carnitina/metabolismo , Dieta Hiperlipídica , Suplementos Nutricionais , Fator de Crescimento Insulin-Like I/química , Ratos , Ratos Sprague-Dawley , Aumento de PesoRESUMO
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 1H NMR, 13C 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.
Assuntos
Acetilcolinesterase/metabolismo , Anidrase Carbônica II/antagonistas & inibidores , Anidrase Carbônica I/antagonistas & inibidores , Inibidores da Anidrase Carbônica/farmacologia , Inibidores da Colinesterase/farmacologia , Imidazóis/farmacologia , Anidrase Carbônica I/metabolismo , Anidrase Carbônica II/metabolismo , Inibidores da Anidrase Carbônica/síntese química , Inibidores da Anidrase Carbônica/química , Inibidores da Colinesterase/síntese química , Inibidores da Colinesterase/química , Relação Dose-Resposta a Droga , Humanos , Imidazóis/síntese química , Imidazóis/química , Simulação de Acoplamento Molecular , Estrutura Molecular , Sais/síntese química , Sais/química , Sais/farmacologia , Relação Estrutura-AtividadeRESUMO
In this study, a series of novel bis-sulfone compounds (2a-2j) were synthesized by oxidation of the bis-sulfides under mild reaction conditions. The bis-sulfone derivatives were characterized by 1 H-NMR, 13 C-NMR, Fourier-transform infrared spectroscopy, and elemental analysis techniques. Nuclear Overhauser effect experiments were performed to determine the orientation of the sulfonyl groups in bis-sulfone derivatives. Here, we report the synthesis and testing of novel bis-sulfone compound-based hybrid scaffold of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibitors for the development of novel molecules toward the therapy of Alzheimer's disease. The novel synthesized bis-sulfone compounds demonstrated Ki values between 11.4 ± 3.4 and 70.7 ± 23.2 nM on human carbonic anhydrase I isozyme (hCA I), 28.7 ± 6.6 to 77.6 ± 5.6 nM on human carbonic anhydrase II isozyme (hCA II), 18.7 ± 2.61 to 95.4 ± 25.52 nM on AChE, and 9.5 ± 2.1 to 95.5 ± 1.2 nM on BChE enzymes. The results showed that novel bis-sulfone derivatives can have promising drug potential for glaucoma, leukemia, epilepsy, and Alzheimer's disease, which are associated with the high enzymatic activity of hCA I, hCA II, AChE, and BChE enzymes.
Assuntos
Acetilcolinesterase/química , Butirilcolinesterase/química , Anidrase Carbônica II/antagonistas & inibidores , Anidrase Carbônica I/antagonistas & inibidores , Inibidores da Anidrase Carbônica/química , Inibidores da Colinesterase/química , Cicloexanonas/química , Sulfonas/química , Doença de Alzheimer/enzimologia , Humanos , Imageamento por Ressonância Magnética , Conformação Proteica , Espectroscopia de Infravermelho com Transformada de Fourier , Relação Estrutura-AtividadeRESUMO
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 13C NMR, 1H 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 α-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⯱â¯0.33-22.51⯱â¯8.59â¯nM against hCA I, 13.77⯱â¯2.21-30.81⯱â¯4.87â¯nM against hCA II, 0.44⯱â¯0.08-1.87⯱â¯0.11â¯nM against AChE and 3.25⯱â¯0.34-12.89⯱â¯4.77â¯nM against BChE. Additionally, we studied the inhibition effect of these derivatives on aldose reductase and α-glycosidase enzymes. For these compounds, compound 1d showed maximum inhibition effect against AR with a Ki value of 360.37⯱â¯55.82â¯nM. Finally, all compounds were tested for the inhibition of α-glycosidase enzyme, which recorded efficient inhibition profiles with Ki values in the range of 4.44⯱â¯0.65-12.67⯱â¯2.50â¯nM against α-glycosidase.
Assuntos
Aminopiridinas/química , Complexos de Coordenação/química , Inibidores Enzimáticos/química , Aminopiridinas/síntese química , Complexos de Coordenação/síntese química , Cristalografia por Raios X , Ensaios Enzimáticos , Inibidores Enzimáticos/síntese química , Humanos , Ligantes , Paládio/químicaRESUMO
Enantioselective synthesis of functionalized cyclic allylic alcohols via kinetic resolution in transesterifcation with different lipase enzymes has been developed. The influence of the enzymes and temperature activity was studied. By determination of ideal reaction conditions, byproduct formation is minimized; this made it possible to prepare enantiomerically enriched allylic alcohols in high ee's and good yields. Enantiomerically enriched allylic alcohols were used for enantiomerically enriched oxazolidinone synthesis. Using benzoate as a leaving group means that 1â¯mol % of potassium osmate is necessary and can be obtained high yields 98%. Inhibitory activities of enantiomerically enriched oxazolidinones (8, 10 and 12) were tested against human carbonic anhydrase I and II isoenzymes (hCA I and hCA II), acetylcholinesterase (AChE), and α-glycosidase (α-Gly) enzymes. These enantiomerically enriched oxazolidinones derivatives had Ki values in the range of 11.6⯱â¯2.1-66.4⯱â¯22.7â¯nM for hCA I, 34.1⯱â¯6.7-45.2⯱â¯12.9â¯nM for hCA II, 16.5⯱â¯2.9 to 35.6⯱â¯13.9 for AChE, and 22.3⯱â¯6.0-70.9⯱â¯9.9â¯nM for α-glycosidase enzyme. Moreover, they had high binding affinity with -5.767, -6.568, -9.014, and -8.563â¯kcal/mol for hCA I, hCA II, AChE and α-glycosidase enzyme, respectively. These results strongly supported the promising nature of the enantiomerically enriched oxazolidinones as selective hCA, AChE, and α-glycosidase inhibitors. Overall, due to these derivatives' inhibitory potential on the tested enzymes, they are promising drug candidates for the treatment of diseases like glaucoma, leukemia, epilepsy; Alzheimer's disease; type-2 diabetes mellitus that are associated with high enzymatic activity of CA, AChE, and α-glycosidase.
Assuntos
Inibidores Enzimáticos/farmacologia , Simulação de Acoplamento Molecular , Oxindóis/farmacologia , Propanóis/química , Acetilcolinesterase/metabolismo , Anidrases Carbônicas/metabolismo , Relação Dose-Resposta a Droga , Inibidores Enzimáticos/síntese química , Inibidores Enzimáticos/química , Glicosídeo Hidrolases/antagonistas & inibidores , Glicosídeo Hidrolases/metabolismo , Humanos , Isoenzimas/antagonistas & inibidores , Isoenzimas/metabolismo , Estrutura Molecular , Oxindóis/síntese química , Oxindóis/química , Estereoisomerismo , Relação Estrutura-AtividadeRESUMO
In this paper, a series of novel bromophenol derivatives were synthesized and evaluated for their acetylcholinesterase and α-glycosidase enzymes inhibition properties and antioxidant activity. Diarylmethanones were synthesized and their bromination was carried out. During bromination, some compounds gave new bromophenols via regioselective O-demethylation. Demethylation of brominated diarylmethanones was also performed with BBr3 to give novel bromophenols. In addition, we examines the antioxidant capacity of novel bromophenol derivatives using several in vitro bioanalytical methodologies such as 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTSâ +) and 1,1-diphenyl-2-picryl-hydrazyl free radical (DPPH) radical scavenging activity, Fe3+ and Cu2+ reducing activities and ferrous (Fe2+) ions chelating activities. Also, novel bromophenols and methoxylated bromophenols derivatives were tested against acetylcholinesterase and α-glycosidase, which associated with some metabolic diseases. The novel bromophenols showed Ki values in range of 8.94⯱â¯0.73-59.45⯱â¯14.97â¯nM against AChE and 4.31⯱â¯1.93-44.14⯱â¯2.19â¯nM against α-glycosidase.
Assuntos
Antioxidantes/farmacologia , Antagonistas Colinérgicos/farmacologia , Inibidores Enzimáticos/farmacologia , Hipoglicemiantes/farmacologia , Bifenil Polibromatos/farmacologia , Acetilcolinesterase/metabolismo , Animais , Antioxidantes/síntese química , Antioxidantes/química , Benzotiazóis/antagonistas & inibidores , Compostos de Bifenilo/antagonistas & inibidores , Antagonistas Colinérgicos/síntese química , Antagonistas Colinérgicos/química , Relação Dose-Resposta a Droga , Enguias , Inibidores Enzimáticos/síntese química , Inibidores Enzimáticos/química , Glicosídeo Hidrolases/metabolismo , Hipoglicemiantes/síntese química , Hipoglicemiantes/química , Estrutura Molecular , Picratos/antagonistas & inibidores , Bifenil Polibromatos/síntese química , Bifenil Polibromatos/química , Relação Estrutura-Atividade , Ácidos Sulfônicos/antagonistas & inibidoresRESUMO
In the presence of chiral organic catalysts, the optically active 4H-chromine was synthesized from the multicomponent condensation of 5,5-dimethylcyclohexane-1,3-dione with malononitrile and methylene-active compound, and the specific angle of rotation of the compounds was determined in the AUTOPOL-III polarimeter and their structures were confirmed by the X-ray spectroscopic analysis method. These optically active 2-amino-4-aryl-7,7-dimethyl-5-oxo-5,6,7,8-tetrahydro-4H-chromen-3-carbonitriles were effective inhibitors of α-glycosidase, the cytosolic carbonic anhydrase I and II isoforms (hCA I and II), and acetylcholinesterase (AChE) enzymes with Ki values in the range of 21.33 ± 1.11 to 40.24 ± 10.78 µM for hCA I, 28.91 ± 6.51 to 59.97 ± 15.62 µM for hCA II, 18.16 ± 3.18 to 66.57 ± 1.36 µM for α-glycosidase, and 8.68 ± 0.93 to 102.61 ± 24.96 µM for AChE.
Assuntos
Anticonvulsivantes/farmacologia , Antagonistas Colinérgicos/farmacologia , Hipoglicemiantes/farmacologia , Nitrilas/farmacologia , Anticonvulsivantes/síntese química , Anticonvulsivantes/química , Antagonistas Colinérgicos/síntese química , Antagonistas Colinérgicos/química , Cristalização , Humanos , Hipoglicemiantes/síntese química , Hipoglicemiantes/química , Nitrilas/síntese química , Nitrilas/química , Relação Estrutura-AtividadeRESUMO
A novel class of fluoro-substituted tris-chalcones derivatives (5a-5i) was synthesized from phloroglucinol and corresponding benzaldehydes. A three step synthesis method was followed for the production of these tris-chalcone compounds. The structures of the newly synthesized compounds (5a-5i) were confirmed on the basis of IR, 1H NMR, 13C NMR, and elemental analysis.The compounds' inhibitory activities were tested against human carbonic anhydrase I and II isoenzymes (hCA I and hCA II), acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and α-glycosidase (α-Gly). These chalcone derivatives had Ki values in the range of 19.58-78.73â¯nM for hCA I, 12.23-41.70â¯nM for hCA II, 1.09-6.84â¯nM for AChE, 8.30-32.30â¯nM for BChE and 0.93⯱â¯0.20-18.53⯱â¯5.06â¯nM against α-glycosidase. These results strongly support the promising nature of the tris-chalcone scaffold as selective carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, and α-glycosidase inhibitor. Overall, due to these derivatives' inhibitory potential on the tested enzymes, they are promising drug candidates for the treatment of diseases like glaucoma, leukemia, epilepsy; Alzheimer's disease; type-2 diabetes mellitus that are associated with high enzymatic activity of carbonic anhydrase, acetylcholine esterase, butyrylcholinesterase, and α-glycosidase.
Assuntos
Inibidores da Anidrase Carbônica/química , Chalconas/química , Inibidores da Colinesterase/química , Inibidores de Glicosídeo Hidrolases/química , Acetilcolinesterase/química , Butirilcolinesterase/química , Anidrase Carbônica I/química , Anidrase Carbônica II/química , Inibidores da Anidrase Carbônica/síntese química , Chalconas/síntese química , Inibidores da Colinesterase/síntese química , Inibidores de Glicosídeo Hidrolases/síntese química , Humanos , Estrutura MolecularRESUMO
During this investigation, N,N'-bis-azidomethylamines, N,N'-bis-cyanomethylamine, new alkoxymethylamine and chiral derivatives, which are considered to be a new generation of multifunctional compounds, were synthesized, functional properties were investigated, and anticholinergic and antidiabetic properties of those compounds were studied through the laboratory tests, and it was approved that they contain physiologically active compounds rather than analogues. Novel N-bis-cyanomethylamine and alkoxymethylamine derivatives were effective inhibitors of the α-glycosidase, cytosolic carbonic anhydrase I and II isoforms, butyrylcholinesterase (BChE), and acetylcholinesterase (AChE) with Ki values in the range of 0.15-13.31 nM for α-glycosidase, 2.77-15.30 nM for human carbonic anhydrase isoenzymes I (hCA I), 3.12-21.90 nM for human carbonic anhydrase isoenzymes II (hCA II), 23.33-73.23 nM for AChE, and 3.84-48.41 nM for BChE, respectively. Indeed, the inhibition of these metabolic enzymes has been considered as a promising factor for pharmacologic intervention in a diversity of disturbances.
Assuntos
Inibidores da Anidrase Carbônica , Inibidores da Colinesterase , Inibidores de Glicosídeo Hidrolases , Animais , Inibidores da Anidrase Carbônica/síntese química , Inibidores da Anidrase Carbônica/química , Inibidores da Colinesterase/síntese química , Inibidores da Colinesterase/química , Inibidores de Glicosídeo Hidrolases/síntese química , Inibidores de Glicosídeo Hidrolases/química , HumanosRESUMO
Compounds containing nitrogen and sulfur atoms can be widely used in various fields, including industry, medicine, biotechnology, and chemical technology. Among them, amides of acids and heterocyclic compounds have an important place. These amides and thiazolidine-4-ones showed good inhibitory action against butyrylcholinesterase (BChE), acetylcholinesterase (AChE), and human carbonic anhydrase isoforms. AChE exists at high concentrations in the brain and red blood cells. BChE is an important enzyme that is plentiful in the liver, and it is released into the blood in a soluble form. They were demonstrated to have effective inhibition profiles with Ki values of 23.76-102.75 nM against hCA I, 58.92-136.64 nM against hCA II, 1.40-12.86 nM against AChE, and 9.82-52.77 nM against BChE. On the other hand, acetazolamide showed Ki value of 482.63 ± 56.20 nM against hCA I, and 1019.60 ± 163.70 nM against hCA II. Additionally, Tacrine inhibited AChE and BChE, showing Ki values of 397.03 ± 31.66 and 210.21 ± 15.98 nM, respectively.