Investigation of Inhibition Effects of Some Natural Phenolic Compounds on Glutathione S-transferase (GST), Acetylcholinesterase (AChE), Butyrylcholinesterase (BChE), [alpha]-Amylase, and [alpha]-Glycosidase: Antidiabetic, Anticholinergics, Antiparasitic study.
Summary: Herein, we report the experimental results of the inhibition effects of some phenolic compounds such as 2,4,6-Trihydroxybenzaldehyde, 3,4-Dihydroxy-5-methoxybenzoic acid, Serotonin hydrochloride on [alpha]-amylase, [alpha]-glycosidase, acetylcholinesterase (AChE), butyrylcholinesterase (BChE) and glutathione S-transferase (GST) enzymes. [alpha]-Amylase from porcine pancreas, [alpha]-glycosidase from Saccharomyces cerevisiae, glutathione s-transferase from human placenta, acetylcholinesterase from human erythrocytes and Butyrylcholinesterase from equine serum were used as enzymes. These enzymes play a very important role in metabolism. In this study the Ki values obtained by the experiments done for the compounds on some enzymes such as GST, AChE, BChE, [alpha]-amylase and [alpha]-glycosidase were found in the range of 0.31+-0.5-1.02+-0.3 uM, 484.03+-45.45-802.83+-104.3 uM, 238.22+-67.31-482.73+-125.6 uM and 9.28+-0.56-11.23+-3.43 uM, respectively.
The experiment results showed that the [alpha]-amylase enzyme has a selective inhibitory effect and its IC50 values were found to be in the range of 0.92-9.63 uM. As a result, it was found that these phenolic compounds have a selective effect on [alpha]-amylase, [alpha]-glycosidase, AChE, BChE and GST enzymes, and they can be used as antiparasitic, antidiabetic and anticholinergic.
Keywords: Phenolic compounds; Enzyme inhibition; [alpha]-glycosidase; [alpha]-amylase; Acetylcholinesterase; Glutathione s-transferase.
Antioxidant compounds play an important role in health care to prevent and scavenge free radicals; degenerative ailments and alleviate chronic diseases such as autoimmune disorders, cancer, atherosclerosis, hypertension, and delay the ageing process [1, 2]. Serotonin hydrochloride is a main neurotransmitter and affects diverse functions both in the brain and in the rest of the body. 3,4 Dihydroxy-5-methoxybenzoic acid can be synthesized using a simple method with methyl gallate and using an advanced method taking ethyl gallate .
Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes are significant enzymes that catalyze the breakdown of acetylcholine (ACh) and some other choline ester molecules that function as neurotransmitter molecules, which are recorded as drug purposes for Alzheimer's disease (AD).
Acetylcholinesterase compounds can act as inhibitors. Therefore, these compounds have been used in the treatment of rheumatic some disorders such as alzheimer, myasthenia gravis and glaucoma. Also, cholinesterase inhibitor compounds are extensively utilized as pesticides and, if misused, can produce toxic responses in human and mammals [4-6].
Glutathione-S-transferase (GST; EC 18.104.22.168) enzyme hydrolyzes the nucleophilic moieties of glutathione and this hydrolysis process results in various electrophilic products. Additionally, glutathione has a very important role in the detoxification process in mammal cells and in some process herbicides of plant cells [7, 8].
Diabetes mellitus is categorized as an insulin-independent disease (T2DM) due to some factors such as a low biological activity of occult insulin, a reduced insulin secretion from pancreatic [beta]-cells, and insulin affiliate (T1). Excessive defects in type 2 diabetic diseases cause insulin cells to become unresistant. As a result, the insulin signal channel is perturbed and thus, the absorption of glucose in tissues such as muscle is impaired .
[alpha]-Amylase and [alpha]-glucosidase enzyme molecules ensure the hydrolysis of carbohydrate molecules. Hence, the digestion of glucose molecules is facilitated. The resulting glucose molecules are more easily passed into the bloodstream. In this study, [alpha]-amylase and [alpha]-glucosidase enzyme molecules have been used as antidiabetic ordinary medicine. These compounds provide a protection against disease-causing effects; hence, they are highly effective in growth and reproduction.
Additionally, the phenolic compounds give electrons or atoms to free radicals. As a result, reactive oxygen species (ROS) and other free radicals present in living organism are removed. [alpha]-Glycosidase is an important catalytic enzyme and it annihilates the complex carbohydrate molecules into simple absorbable sugar units [9-11].
Herein, we investigated the in vitro inhibition effects of 2,4,6-trihydroxybenzaldehyde, 3,4-dihydroxy-5-methoxybenzoic acid, Serotonin hydrochloride compounds on GST, AChE, BChE, [alpha]-glycosidase and [alpha]-amylase enzymes. In the current study, starch solution and p-nitrophenyl-D-glucopyranoside compound were used as substrates for [alpha]-amylase and [alpha]-glycosidase enzymes, respectively.
[alpha]-Amylase enzyme obtained from pig pancreas (Type IV-B, Sigma-Aldrich A3176, St. Louis, MO, USA) and [alpha]-glycosidase obtained from Saccharomyces cerevisiae (Tipe I, Sigm-Aldrich G5003, St. Louis, MO, USA) were purchased from Sigma Aldrich. These enzymes are commercially present, used without any further purification in the study. Glutathione, strach, used for GST and p-nitrophenyl-[alpha]-D-glycopiranoside (Sigma-Aldrich, N1377-1G, St. Louis, MO, USA) were used as for GST, [alpha]-amylase and [alpha]-glycosidase, respectively.
50% bacterial strains and 1-chloro-2,4-dinitrobenzene (CDNB) compound as a substrate were used in the experiments done to determine GST activity. The results showed that GST has a high activity in bacteria compared to fungi, algae, and protozoa. A buffer phosphate solution (pH 6.5), GST (20 mM) solution and CDNB (25 mM) solution were prepared to perform the GST activity. Each test was taken at 340 nm absorbance for 3 minutes with a spectrophotometer .
[alpha]-glycosidase enzyme activity was performed with p-nitrophenyl-D-glycopyranoside (p-NPG) as the substrate according to explained elsewhere . Briefly, a 200 uL phosphate buffer (PB) solution (0.15 U/mL, pH 7.4) was prepared, and then 40 uL homogenate solution was added to this buffer solution. After pre-incubation, 50 uL of p-NPG (5 mM, pH 7.4) was added to the resultin solution. The temperature was brought to 30 AdegC and the solution was incubated again. The absorbance measurements were performed at 405 nm as in previous studies. The IC50 value of activity (%) was calculated as compared to the concentration of plant concentration [14, 15].
[alpha]-Amylase activity was determined according to the methodology recorded by Xiao et al.  In this paper, dissolve 6 g of starch solution in 240 ml of NaOH 0.4 M and warm up to 70 Adeg C for 25 minutes. Also, in ice water, with 2.0 M HCl, the pH of the solution was adjusted to 6.9 and H2O was added to 300 ml. Sample solutions were prepared by dissolving 5 mg in 5 mL (EtOH: H2O). In the presence of total enzyme inhibition, several solutions were prepared in phosphate buffer. Buffer solution (pH: 5), phosphate buffer solution (pH 6.9, 100 uL) and dissolved solutions (200-500 uL) were mixed and then placed at 37 Adeg C for 30 minutes. Then, 10 mL of the enzyme solution was added 50 ug / mL and it was incubated for 30 minutes. Absorption was measured by spectrophotometry at 580 nm. One unit of [alpha]-amylase enzyme is the amount of enzyme that liberates 1.0 milligrams of starch maltose in 3 minutes at pH 6.9 at 20 Adeg C .
AChE/BChE activity determination and inhibition studies
AChE/BChE inhibitory effect of phenolic compounds was measured according to Ellman et al. . Butyrylthiocholine iodide (BChI), as well as acetylthiocholine iodide (AChI) molecules were utilized as substrate compounds of the reaction. In this section, 5,5'-Dithio-bis (2-nitro-benzoic acid) compound (DTNB) was used to estimate BChE / AChE activity. In summary, 100 uL Tris buffer solution (HCl, 1.0 M, pH 8.0, Tris) and a variety of concentration of sample solution (50 to 200 mL) in deionized water to 20 uL of BChE/AChE enzymes solutions. The mixture is then incubated for 10 minutes at 20 Adeg C. Finally, 50 uL of DTNB (0.5 mM and 25 mL) BChI / AChI were added to the incubator mixture. The reaction was also started by adding 50 uL BChI / AChI. The activity of these enzymes was evaluated using spectrophotometric spectra with a wavelength of 412 nm. [19-21].
Results and discussion
Herein; [alpha]-amylase, [alpha]-glycosidase, AChE, BChE and GST were used as enzyme inhibitors. For this purpose, some phenolic compounds were taken and studied to reveal their inhibition effects on GST, [alpha]-glycosidase, [alpha]-amylase, AChE, and BChE. As given below, the results of experiments showed that phenolic compounds have an effective inhibition. Some chemical properties of phenolic compounds are given in Fig 2, and the results of inhibition experiments are given in Table-1.
The GST enzymes lead to an increase of resistance to factors that cause chemotherapy. The findings of this study are summarized as below:
1. The IC50 value of [alpha]-amylase, a natural phenolic compound, was found in the range of 0.92-9.63 uM. IC50 values (as seen in Table 1) found for acarbose which is a phenolic compound and has a positive effect were found as: Serotonin hydrochloride (0.92 uM, r2: 0.9730) < 2,4,6-Trihydroxybenzaldehyde (1.84 uM, r2: 0.9823) < 3,4-Dihydroxy-5-methoxybenzoic acid (9.63 uM, r2: 0.9773) < Acarbose (10 uM).
2. The evaluation of inhibitory effect of [alpha]-glycosidase on the phenolic compounds showed that the IC50 values of this phenolic compound are changed in the range of 9.28+-0.56-11.23+-3.43 uM as seen in Table 1 and Fig 4. IC50 values of acarbose as a standard molecul and phenolic compounds for [alpha]-glycosidase were changed the following order: 2,4,6-Trihydroxybenzaldehyde (13.74 uM, r2: 0.9488) < 3,4-Dihydroxy-5-methoxybenzoic acid (14.03 uM, r2: 0.9309) < Serotonin hydrochloride (15.93 uM, r2: 0.9823) < Acarbose (22.800 uM). On the other hand, Ki values of compound exhibited the following order: 3,4-Dihydroxy-5-methoxybenzoic acid (9.28+-0.56 uM) < 2,4,6-Trihydroxybenzaldehyde (10.93+-1.34 uM) a Serotonin hydrochloride (11.23+-3.43 uM) < Acarbose (22.800 uM).
3. IC50 values for AChE compound were found to be in the range of 608.34-943.03 uM, and Ki values of AChE compound were found to be in the range of 484.03+-45.45-802.83+-104.3 uM. IC50 values of acarbose as a standard molecule and phenolic compounds for AChE compound were changed as: 3,4-Dihydroxy-5-methoxybenzoic acid (608.34 uM, r2: 0.9384) < 2,4,6-Trihydroxybenzaldehyde (843.83 uM, r2: 0.9384) < Serotonin hydrochloride (943.03 uM, r2: 0.9730) < Acarbose (22800 uM). IC50 values of BChE were found to be in the range of 304.64+-523.94, and Ki values of BChE were found to be in the range of 238.22+-67.31-482.73+-125.6 uM. IC50 values of acarbose as a standard molecul and phenolic compounds for BChE were changed the following order: 3,4-Dihydroxy-5-methoxybenzoic acid (304.64 uM, r2: 0.9424) < Serotonin hydrochloride (484.03 uM, r2: 0.9538) < 2,4,6-Trihydroxybenzaldehyde (523.94 uM, r2: 0.9589) < Acarbose (22800 uM).
4. Ki values of GST, as natural phenolic molecule, were found to be in the range of 0.31+-0.5-1.02+-0.3 uM. The highest inhibition effect was detected with 2,4,6-Trihydroxybenzaldehyde having 8.34+-1.10 uM of Ki as given in Fig 3. IC50 values of phenolic compounds for GST were found as: 2,4,6-Trihydroxybenzaldehyde (0.24 uM, r2: 0.9904) < Serotonin hydrochloride (0.38 uM, r2: 0.9648) < 3,4-Dihydroxy-5-methoxybenzoic acid (0.97 uM, r2: 0.9947).
Table-1: Inhibition constants (Ki) and half maximal inhibition concentration (IC50) values obtained experiments done with natural phenolic compounds against [alpha]-amylase, [alpha]-glycosidase, AChE, BChE, and GST enzymes.
###R2###R2###Ki (uM)###R2###Ki (uM)###R2
###Ki (nM)###R2###Ki (nM)
The inhibitor compounds of [alpha]-amylase enzyme have not only the beneficial effect on the postprandial glycemia but also a beneficial action against viral agents and arterial hypertension. Recent scientific researches show that different substances isolated from the plant tissues have a very important hypoglycemiant efficacy [22, 23]. The compounds having an inhibitory effect of and-amilaz are present in some agents which are used for some applications such as crop protection and diabetes treatment. Diabetes is considered the basis of today's health issues, and it is a metabolic disorder caused by high glucose levels in blood. Many diseases such as high blood pressure, cardiovascular disease, gangrene, weakness, neuropathy and nephropathy retinopathy occur in the human body due to diabetes . The compounds of [alpha]-Glycosidase that having an inhibitory effect can play an important role in therapeutic modality (T2DM).
Postprandial hyperglycemia disease is an important symptom in the early diagnosis and diagnosis of diabetic diseases. Control of blood levels due to postprandial hyperglycemia disease is effective in preventing the occurrence of a second disorder . [alpha]-Glycosidase inhibitor drugs are oral and anti-diabetic. These drugs affect the conversion of carbohydrates to mono sugars and accordingly affect the regulation of carbohydrate digestion . Firstly, the cholinergic hypothesis was used to identify AD. In this case, it was concluded that the ACh compound formed in neuron cells prevented hydrolysis and prevented synaptic depression [27-31]. Thanks to AChE inhibitor affect, the hydrolysis of ACh is blocked. In addition, designing and regulating the inhibitor compound for the AChE enzyme is effective in preventing the formation of AD. Commercial drugs of galatamine, donepezil and rivastigm approved by the FDA have aroused great interest [32-38].
The GST enzyme is clearly present in the liver tissue, but is also observed in brain, kidney, retina, eye lens, lung tissues and placenta . Liver is an important tissue and it contains poisonous objects such as ionic metals, carcinogenic metabolites, toxic chemicals, drugs and some endogenous toxic compounds of plant origin .
The inhibition effects of drugs used in this study on GST enzyme were given as seen in Table 1, and then evaluated. Also, Table 1 shows Ki and IC50 values found for tested compounds in this work.
In this study, we report the effect of 2,4,6-Trihydroxybenzaldehyde., 3,4-Dihydroxy-5-methoxybenzoic acid, Serotonin hydrochloride phenolic compounds (seen in Table 1) on GST, AChE, BChE, [alpha]-amylase and [alpha]-glycosidase enzyme activities. The experiment results revealed that IC50 values tested with the whole compounds for GST, [alpha]-amylase and [alpha]-glycosidase enzymes were found to be micromolar level, but IC50 values tested with the whole compounds for AChE and BChE enzymes were detected to be nanomolar levels. These results show that these phenolic compounds tested in the study have a selective effect for GST, [alpha]-amylase and [alpha]-glycosidase enzymes. [alpha]-Glycosidase drugs are known as the factors affecting the therapeutic effect of some diseases such as obesity, hyperglycemia and type II-independent DM. Recently, GST inhibitors have also emerged among the therapeutic factors for providing resistance for anticancer agents.
GST inhibitors are important lead compounds which are used in both anti-parasite drugs and drug diagnosis. [alpha]-amylase molecules bound to long chain carbohydrate chains are broken down into glucose monosaccharides by decomposition of starch and dissaccharides with [alpha]-glycosidase. [alpha]-Glucosidase inhibitors have been shown to have promising antiviral and antitumor effects.
Conflict of Interest
The authors declare that there are no conflicts of interest.
1. I. Gulcin, R. Elias, A. Gepdiremen and L. Boyer, Antioxidant activity of lignans from fringe tree (Chionanthus virginicus L.), Euro. Food Research Tec., 223, (2006).
2. I. Gulcin, Comparison of in vitro antioxidant and antiradical activities of L-tyrosine and L-Dopa, Amino Acids, 32, (2007).
3. I. Gulcin, M. Elmastas and H. Y. Aboul-Enein, Determination of antioxidant and radical scavenging activity of basil (Ocimum basilicum) assayed by different methodologies, Phytotherapy Research, 21, 4 (2007).
4. N. OztasA,kin, Y. CA,etinkaya, P. Taslimi, S. Goksu and I. GulcA,in, Antioxidant and acetylcholinesterase inhibition properties of novel bromophenol derivatives, Bioorg. Chem., 60, 49 (2015).
5. A. Sujayev, E. Garibov, P. Taslimi, I. Gulcin, S. Gojayeva, V. Farzaliyev, S. H. Alwasel and C. T. Supuran, Synthesis of some tetrahydropyrimidine-5-carboxylates, determination of their metal chelating effects and inhibition profiles against acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase, J. Enzyme Inhib. Med. Chem., 31, 6 (2016).
6. I. Gulcin, A. Scozzafava, C. T. Supuran, Z. Koksal, F. Turkan, S. Cetinkaya, Z. Bingol, Z. Huyut and S. H. Alwasel, The effect of caffeic acid phenethyl ester (CAPE) on metabolic enzymes including acetylcholinesterase, butyrylcholinesterase, glutathione S-transferase, lactoperoxidase, and carbonic anhydrase isoenzymes I, II, IX, and XII, J. Enzyme Inhib. Med. Chem., 31, 6 (2016).
7. F. Turkan, Z. Huyut and M. N. Atalar, The toxicologial impact of some avermectins on human erythrocytes glutathione S-transferase enzyme, J. Biochem. Mol. Toxicol., 32, 10 (2018).
8. I. Gulcin, A. Scozzafava, C.T. Supuran, H. Akincioglu, Z. Koksal, F. Turkan and S. Alwasel, Rosmarinic acid inhibits some metabolic enzymes including glutathione S-transferase, lactoperoxidase, acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase isoenzymes, J. Enzyme Inhib. Med. Chem., 31, 6 (2016).
9. P. Taslimi, C. Caglayan, V. Farzaliyev, O. Nabiyev, A. Sujayev, F. Turkan, R. Kaya and I. GulcA,in, Synthesis and discovery of potent carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase and [alpha]-glycosidase enzymes inhibitors: the novel N, N'-bis-cyanomethylamine and alkoxymethylamine derivatives, J. Biochem. Mol. Toxicol. 32, 4 (2018).
10. S. Burmaoglu, A.O. Yilmaz, P. Taslimi, O. Algul, D. Kilic and I. GulcA,in, Synthesis and biological evaluation of phloroglucinol derivatives possessing [alpha]-glycosidase, acetylcholinesterase, butyrylcholinesterase, carbonic anhydrase inhibitory activity, Arch. der pharm., 351, 2 (2018).
11. F. Erdemir, D. Barut Celepci, A. Aktas, P. Taslimi, Y. Gok, H. Karabiyik and I. GulcA,in, 2-Hydroxyethyl substituted NHC precursors: Synthesis, characterization, crystal structure and carbonic anhydrase, [alpha]-glycosidase, butyrylcholinesterase, and acetylcholinesterase inhibitory properties, J. Mol Struct., 1155, (2018).
12. H. E. Aslan, Y. Demir, M. S. Ozaslan, F. Turkan, S. Beydemir and O. I. Kufrevioglu, The behavior of some calcones on acetylcholinesterase and carbonic anhydrase activity, Drug Chem. Toxicol., https://doi.org/10.1080/01480545.2018.1 463242.
13. Y. Tao, Y. Zhang and Y. Cheng, Rapid screening and identification of [alpha]-glucosidase inhibitors from mulberry leaves using enzyme-immobilized magnetic beads coupled with HPLC/MS and NMR, Biomed. Chrom., 27, (2013).
14. P. Taslimi H. Akincioglu and I. GulcA,in, Synephrine and phenylephrine act as [alpha]-amylase, [alpha]-glycosidase, acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase enzymes inhibitors, J. Biochem. Mol. Toxicol., 31, 11 (2017).
15. P. Taslimi, C. Caglayan and Y. GulcA,in, The impact of some natural phenolic compounds on carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, and a-glycosidase enzymes: an antidiabetic, anticholinergic, and antiepileptic study, J. Biochem. Mol. Toxicol., 31, 12 (2017).
16. Z. Xiao, R. Storms and A. A. Tsang, Quantitative starch-iodine method for measuring alpha-amylase and glucoamylase activities, Anal. Biochem., 351 (2006).
17. I. GulcA,in, P. Taslimi, A. Aygun, S. Nastaran, E. Bastem O. I. Kufrevioglu, F. Turkan and F.Sen, Antidiabetic and antiparasitic potentials: Inhibition effects of some natural antioxidant compounds on [alpha]-glycosidase, [alpha]-amylase and human glutathione S-transferase enzymes, Int J Biol Macromol., 119, (2018).
18. G. L. Ellman, K. D. Courtney, V. Andres and R. M. Featherston, A new and rapid colorimetric determination of acetylcholinesterase activity, Biochem. Pharmacol., 7, (1961).
19. F. Turkan, Z. Huyut, P. Taslimi and I. GulcA,in, The in vivo effects of cefazolin, cefuroxime, and cefoperazon on the carbonic anhydrase in different rat tissues, J. Biochem. Mol. Toxicol., 32, 3 (2018).
20. F. Turkan, Z. Huyut, P. Taslimi and I. GulcA,in, The effects of some antibiotics from cephalosporin groups on the acetylcholinesterase and butyrylcholinesterase enzymes activities in different tissues of rats, Arch. Physiol. Biochem. 125, 1 (2018).
21. C. Yamali, H. I. Gul, A. Ece, P. Taslimi and I. GulcA,in, Synthesis, molecular modeling and biological evaluation of 4-[5-aryl-3-(thiophen-2-yl)-4, 5-dihydro-1H-pyrazol-1-yl]benzenesulfonamides towards acetylcholinesterase, carbonic anhydrase I and II enzymes, Chem. Biol. Drug Design., 91, 4 (2018).
22. H. Lineweaver and D. Burk, The Determination of Enzyme Dissociation Constants, J. Am. Chem. Soc., 56, (1934).
23. L. Zhang, S. Hogan and J. R. Li, Grape skin extract inhibits mammalian intestinal a-glucosidase activitand suppresses postprandial glycemic response in streptozocin-treated mice, Food Chem., 126, (2011).
24. F. Hiroyuki, Y. Tomohide and O. Kazunori, Efficacy and safety of Touchi extract, an alpha-glucosidase inhibitor derived from fermented soybeans, in non-insulin-dependent diabetic mellitus, J. Nutr. Biochem., 12, (2001).
25. T. Fujisawa, H. Ikegami and K. Inoue, Effect of two alpha-glucosidase inhibitors, voglibose and acarbose, on postprandial hyperglycemia correlates with subjective abdominal symptoms, Metabolism, 54, (2005).
26. S. Shobana, Y. N. Sreerama and N. G. Malleshi, Composition and enzyme inhibitory properties of finger millet (Eleusine coracana L.) seed coat phenolics: Mode of inhibition of [alpha]-glucosidase and pancreatic amylase, Food Chem., 115, (2009).
27. H. Wang, Y.J. Du and H.C. Song, [alpha]-Glucosidase and [alpha]-amylase inhibitory activities of guava leaves, Food Chem., 123, (2010).
28. P. Taslimi, E. Sujayev, F. Turkan, E. Garibov, Z. Huyut, F. Farzaliyev, S. Mamedova and I. GulcA,in, Synthesis and investigation of the conversion reactions of pyrimidine-thiones with nucleophilic reagent and evaluation of their acetylcholinesterase, carbonic anhydrase inhibition and antioxidant activities, J. Biochem. Mol. Toxicol. 32, 2 (2018).
29. F. Turkan, Z. Huyut, Y. Demir, F. Ertas and S. Beydemir, The effects of some cephalosporins on acetylcholinesterase and glutathione S-transferase: an in vivo and in vitro study, Arch. Physiol. Biochem., 125, 3 (2018).
30. Y. Sari, A. Aktas, P. Taslimi, Y. Gok, C. Caglayan and I. GulcA,in, Novel N-propylphthalimide and 4-vinylbenzyl substituted benzimidazole salts: synthesis, characterization and determination of their metal chelating effects and inhibition profiles against acetylcholinesterase, and carbonic anhydrase enzymes, J. Biochem. Mol. Toxicol., 32, 1 (2018).
31. G. Gondolova, P. Taslimi A. Medjidov, V. Farzaliyev, A. Sujayev, M. Huseynova, O. Sahin, B. Yalcin F. Turkan and I. Gulcin, Synthesis, crystal structure and biological evaluation of spectroscopic characterization of Ni(II) and Co(II) complexes with N-salicyloil-N'-maleoil-hydrazine as anticholinergic and antidiabetic agents, J. Biochem. Mol. Toxicol., 32, 9 (2018).
32. U. M. Kocyigit, S. Durna Dastan, P. Taslimi, T. Dastan and I. GulcA,in, Inhibitory effects of some drugs on carbonic anhydrase enzyme purified from Kangal Akkaraman sheep in Sivas, Turkey, J. Biochem. Mol. Toxicol., 32, 1 (2018).
33. F. Erdemir, D. Barut Celepci, A. Aktas, P. Taslimi, Y. Gok, H. Karabiyik and I. GulcA,in, 2-Hydroxyethyl substituted NHC precursors: Synthesis, characterization, crystal structure and carbonic anhydrase, [alpha]-glycosidase, butyrylcholinesterase, and acetylcholinesterase inhibitory properties, J. Mol. Struct., 1155, (2018).
34. P. Taslimi, S. Osmanova, C. Caglayan, F. Turkan, S. Sardarova, V. Farzaliyev, A. Sujayev N. Sadeghian and I. Gulcin, Novel amides of 1, 1-bis-(carboxymethylthio)-1-arylethanes: Synthesis, characterization, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibitory properties, J. Biochem. Mol. Toxicol., 32, 9 (2018).
35. F. Turkan, Z. Huyut, P. Taslimi, M. T. Huyut and I. GulcA,in, Investigation of the effects of cephalosporin antibiotics on glutathione S-transferase activity in different rat tissues in vivo for drug development research, Drug Chem., Toxicol. https://doi.org/10.1080/01480545.2018.1 497644 (2018).
36. T. Dastan, U. M. Kocyigit, S. D. Dastan, C. Kilickaya, P. Taslimi, C. Ozge, M. Koparir, A. Cetin, C. Orek and I. GulcA,in, Investigation of acetylcholinesterase and mammalian DNA topoisomerases, carbonic anhydrase inhibition profiles and cytotoxic activity of novel bis([alpha]-aminoalkyl)phosphinic acid derivatives against human breast cancer, J. Biochem. Mol. Toxicol., 31, 11 (2017).
37. K. Sato, A. Kitahara, K. Satoh, T. Ishikawa, M. Tatematsu and N. Ito, The placental form of glutathione S-transferase as a new marker protein for preneoplasia in rat chemical hepato-carcinogenesis, Jpn J Cancer Res., 75, 199 (1984).
38. F. Turkan and M. N. Atalar, The effects of amoxicillin and vancomycin hydrochloride hydrate on glutathione S-transferase enzyme activity: An vitro study, Igdir Univ. J. Inst. Sci. and Tech., 8, 2 (2018).
39. M. Torres-Naranjo, A. Suarez and G. Gilardoni, Chemical Constituents of Muehlenbeckia tamnifolia (Kunth) Meisn (Polygonaceae) and Its In Vitro [alpha]-Amilase and [alpha]-Glucosidase Inhibitory Activities, Molcules, 21, (2016).
40. H. Teng, L. Chen and T. Fang, Rb2 inhibits [alpha]-glucosidase and regulates glucose metabolism by activating AMPK pathways in HepG2 cells, J. Funct. Foods., 28, (2017).
|Printer friendly Cite/link Email Feedback|
|Publication:||Journal of the Chemical Society of Pakistan|
|Date:||Aug 31, 2019|
|Previous Article:||The Effects of Some Bis - 1, 2, 4 - Triazole Containing Aminomethyl Derivatives on MDA Levels and Vitamins in Tissues of Rats.|
|Next Article:||Two New Monocyclic Naphthenes from Tamarix indica.|