Publications by authors named "Nastaran Sadeghian"

16 Publications

  • Page 1 of 1

Probing 4-(diethylamino)-salicylaldehyde-based thiosemicarbazones as multi-target directed ligands against cholinesterases, carbonic anhydrases and α-glycosidase enzymes.

Bioorg Chem 2021 Feb 15;107:104554. Epub 2020 Dec 15.

Department of Chemistry, Faculty of Science, Ataturk University, 25240 Erzurum, Turkey.

With the fading of 'one drug-one target' approach, Multi-Target-Directed Ligands (MTDL) has become a central idea in modern Medicinal Chemistry. The present study aimed to design, develop and characterize a novel series of 4-(Diethylamino)-salicylaldehyde based thiosemicarbazones (3a-p) and evaluates their biological activity against cholinesterase, carbonic anhydrases and α-glycosidase enzymes. The hCA I isoform was inhibited by these novel 4-(diethylamino)-salicylaldehyde-based thiosemicarbazones (3a-p) in low nanomolar levels, the Ki of which differed between 407.73 ± 43.71 and 1104.11 ± 80.66 nM. Against the physiologically dominant isoform hCA II, the novel compounds demonstrated Ks varying from 323.04 ± 56.88 to 991.62 ± 77.26 nM. Also, these novel 4-(diethylamino)-salicylaldehyde based thiosemicarbazones (3a-p) effectively inhibited AChE, with Ki values in the range of 121.74 ± 23.52 to 548.63 ± 73.74 nM. For BChE, Ki values were obtained with in the range of 132.85 ± 12.53 to 618.53 ± 74.23 nM. For α-glycosidase, the most effective Ki values of 3b, 3k, and 3g were with Ki values of 77.85 ± 10.64, 96.15 ± 9.64, and 124.95 ± 11.44 nM, respectively. We have identified inhibition mechanism of 3b, 3g, 3k, and 3n on α-glycosidase AChE, hCA I, hCA II, and BChE enzyme activities. Hydrazine-1-carbothioamide and hydroxybenzylidene moieties of compounds play an important role in the inhibition of AChE, hCA I, and hCA II enzymes. Hydroxybenzylidene moieties are critical for inhibition of both BChE and α-glycosidase enzymes. The findings of in vitro and in silico evaluations indicate 4-(diethylamino)-salicylaldehyde-based thiosemicarbazone scaffold to be a promising hit for drug development for multifactorial diseases like Alzheimer's disease.
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http://dx.doi.org/10.1016/j.bioorg.2020.104554DOI Listing
February 2021

Retraction Note: Suppressor capacity of copper nanoparticles biosynthesized using Crocus sativus L. leaf aqueous extract on methadone-induced cell death in adrenal phaeochromocytoma (PC12) cell line.

Sci Rep 2020 Nov 30;10(1):21236. Epub 2020 Nov 30.

Sen Research Group, Department of Biochemistry, University of Dumlupınar, 43000, Kütahya, Turkey.

Editor's Note: this Article has been retracted; the Retraction Note is available at https://doi.org/10.1038/s41598-020-77741-4 .
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http://dx.doi.org/10.1038/s41598-020-77741-4DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7705752PMC
November 2020

Novel quinazolin-sulfonamid derivatives: synthesis, characterization, biological evaluation, and molecular docking studies.

J Biomol Struct Dyn 2020 Nov 23:1-12. Epub 2020 Nov 23.

Department of Chemistry, Faculty of Science, Ataturk University, Erzurum, Turkey.

In the design of novel drugs, the formation of hybrid molecules via the combination of several pharmacophores can give rise to compounds with interesting biochemical profiles. A series of novel quinazolin-sulfonamid derivatives () were synthesized, characterized and evaluated for their antidiabetic, anticholinergics, and antiepileptic activity. These synthesized novel quinazolin-sulfonamid derivatives () were found to be effective inhibitor molecules for the α-glycosidase, human carbonic anhydrase I and II (hCA I and hCA II), butyrylcholinesterase (BChE) and acetylcholinesterase (AChE) enzyme, with Ki values in the range of 100.62 ± 13.68-327.94 ± 58.21 nM for α-glycosidase, 1.03 ± 0.11-14.87 ± 2.63 nM for hCA I, 1.83 ± 0.24-15.86 ± 2.57 nM for hCA II, 30.12 ± 3.81-102.16 ± 13.87 nM for BChE, and 26.16 ± 3.63-88.52 ± 20.11 nM for AChE, respectively. In the last step, molecular docking calculations were made to compare biological activities of molecules against enzymes which are achethylcholinesterase, butyrylcholinesterase and α-glycosidase.Communicated by Ramaswamy H. Sarma.
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http://dx.doi.org/10.1080/07391102.2020.1847193DOI Listing
November 2020

Retraction Note: Novel green synthesis and antioxidant, cytotoxicity, antimicrobial, antidiabetic, anticholinergics, and wound healing properties of cobalt nanoparticles containing Ziziphora clinopodioides Lam leaves extract.

Sci Rep 2020 09 7;10(1):14826. Epub 2020 Sep 7.

Sen Research Group, Biochemistry Department, Faculty of Arts and Science, Dumlupinar University, Evliya Celebi Campus, 43100, Kutahya, Turkey.

Editor's Note: this Article has been retracted; the Retraction Note is available at https://www.nature.com/articles/s41598-020-71843-9.
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http://dx.doi.org/10.1038/s41598-020-71843-9DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7477173PMC
September 2020

Novel green synthesis and antioxidant, cytotoxicity, antimicrobial, antidiabetic, anticholinergics, and wound healing properties of cobalt nanoparticles containing Ziziphora clinopodioides Lam leaves extract.

Sci Rep 2020 07 22;10(1):12195. Epub 2020 Jul 22.

Sen Research Group, Biochemistry Department, Faculty of Arts and Science, Dumlupinar University, Evliya Celebi Campus, 43100, Kutahya, Turkey.

The aim of the experiment was a green synthesis of cobalt nanoparticles from the aqueous extract of Ziziphora clinopodioides Lam (CoNPs) and assessment of their cytotoxicity, antioxidant, antifungal, antibacterial, and cutaneous wound healing properties. The synthesized CoNPs were characterized using different techniques including UV-Vis., FT-IR spectroscopy, X-ray diffraction (XRD), energy dispersive X-ray spectrometry (EDS), scanning electron microscopy (SEM), and transmission electron microscopy (TEM). According to the XRD analysis, 28.19 nm was measured for the crystal size of NPs. TEM and SEM images exhibited a uniform spherical morphology and average diameters of 29.08 nm for the biosynthesized nanoparticles. Agar diffusion tests were done to determine the antibacterial and antifungal characteristics. Minimum inhibitory concentration (MIC), minimum bactericidal concentration (MBC), and minimum fungicidal concentration (MFC) were specified by macro-broth dilution assay. CoNPs indicated higher antibacterial and antifungal effects than many standard antibiotics (p ≤ 0.01). Also, CoNPs prevented the growth of all bacteria at 2-4 mg/mL concentrations and removed them at 2-8 mg/mL concentrations (p ≤ 0.01). In the case of antifungal effects of CoNPs, they inhibited the growth of all fungi at 1-4 mg/mL concentrations and destroyed them at 2-16 mg/mL concentrations (p ≤ 0.01). The synthesized CoNPs had great cell viability dose-dependently and indicated this method was nontoxic. DPPH free radical scavenging test was done to assess the antioxidant potentials, which revealed similar antioxidant potentials for CoNPs and butylated hydroxytoluene. In vivo experiment, after creating the cutaneous wound, the rats were randomly divided into six groups: untreated control, treatment with Eucerin basal ointment, treatment with 3% tetracycline ointment, treatment with 0.2% Co(NO) ointment, treatment with 0.2% Z. clinopodioides ointment, and treatment with 0.2% CoNPs ointment. These groups were treated for 10 days. For histopathological and biochemical analysis of the healing trend, a 3 × 3 cm section was prepared from all dermal thicknesses at day 10. Use of CoNPs ointment in the treatment groups substantially raised (p ≤ 0.01) the wound contracture, hydroxyl proline, hexosamine, hexuronic acid, fibrocyte, and fibrocytes/fibroblast rate and remarkably decreased (p ≤ 0.01) the wound area, total cells, neutrophil, and lymphocyte compared to other groups. In conclusion, CoNPs can be used as a medical supplement owing to their non-cytotoxic, antioxidant, antibacterial, antifungal, and cutaneous wound healing effects. Additionally, the novel nanoparticles (Co(NO) and CoNPs) were good inhibitors of the α-glycosidase, and cholinesterase enzymes.
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http://dx.doi.org/10.1038/s41598-020-68951-xDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7376013PMC
July 2020

Suppressor capacity of copper nanoparticles biosynthesized using Crocus sativus L. leaf aqueous extract on methadone-induced cell death in adrenal phaeochromocytoma (PC12) cell line.

Sci Rep 2020 07 15;10(1):11631. Epub 2020 Jul 15.

Sen Research Group, Department of Biochemistry, University of Dumlupınar, 43000, Kütahya, Turkey.

In this research, we prepared and formulated a neuroprotective supplement (copper nanoparticles in aqueous medium utilizing Crocus sativus L. Leaf aqueous extract) for determining its potential against methadone-induced cell death in PC12. The results of chemical characterization tests i.e., FE-SEM, FT-IR, XRD, EDX, TEM, and UV-Vis spectroscopy revealed that the study showed that copper nanoparticles were synthesized in the perfect way possible. In the TEM and FE-SEM images, the copper nanoparticles were in the mean size of 27.5 nm with the spherical shape. In the biological part of the present research, the Rat inflammatory cytokine assay kit was used to measure the concentrations of inflammatory cytokines. Terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL) test was used to show DNA fragmentation and apoptosis. Caspase-3 activity was assessed by the caspase activity colorimetric assay kit and mitochondrial membrane potential was studied by Rhodamine123 fluorescence dye. Also, the cell viability of PC12 was measured by trypan blue assay. Copper nanoparticles-treated cell cutlers significantly (p ≤ 0.01) decreased the inflammatory cytokines concentrations, caspase-3 activity, and DNA fragmentation and they raised the cell viability and mitochondrial membrane potential in the high concentration of methadone-treated PC12 cells. The best result of neuroprotective properties was seen in the high dose of copper nanoparticles i.e., 4 µg. According to the above results, copper nanoparticles containing C. sativus leaf aqueous extract can be used in peripheral nervous system treatment as a neuroprotective promoter and central nervous system after approving in the clinical trial studies in humans.
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http://dx.doi.org/10.1038/s41598-020-68142-8DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7363853PMC
July 2020

Synthesis, characterization, molecular docking, and biological activities of coumarin-1,2,3-triazole-acetamide hybrid derivatives.

Arch Pharm (Weinheim) 2020 Oct 9;353(10):e2000109. Epub 2020 Jul 9.

Department of Chemistry, Faculty of Science, Ataturk University, Erzurum, Turkey.

Coumarins and their derivatives are receiving increasing attention due to numerous biochemical and pharmacological applications. In this study, a series of novel coumarin-1,2,3-triazole-acetamide hybrids was tested against some metabolic enzymes including α-glycosidase (α-Gly), α-amylase (α-Amy), acetylcholinesterase (AChE), butyrylcholinesterase (BChE), human carbonic anhydrase I (hCA I), and hCA II. The new coumarin-1,2,3-triazole-acetamide hybrids showed K values in the range of 483.50-1,243.04 nM against hCA I, 508.55-1,284.36 nM against hCA II, 24.85-132.85 nM against AChE, 27.17-1,104.36 nM against BChE, 590.42-1,104.36 nM against α-Gly, and 55.38-128.63 nM against α-Amy. The novel coumarin-1,2,3-triazole-acetamide hybrids had effective inhibition profiles against all tested metabolic enzymes. Also, due to the enzyme inhibitory effects of the new hybrids, they are potential drug candidates to treat diseases such as epilepsy, glaucoma, type-2 diabetes mellitus (T2DM), Alzheimer's disease (AD), and leukemia. Additionally, these inhibition effects were compared with standard enzyme inhibitors like acetazolamide (for hCA I and II), tacrine (for AChE and BChE), and acarbose (for α-Gly and α-Amy). Also, those coumarin-1,2,3-triazole-acetamide hybrids with the best inhibition score were docked into the active site of the indicated metabolic enzymes.
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http://dx.doi.org/10.1002/ardp.202000109DOI Listing
October 2020

N-Substituted pyrimidinethione and acetophenone derivatives as a new therapeutic approach in diabetes.

Arch Pharm (Weinheim) 2020 Sep 14;353(9):e2000075. Epub 2020 Jun 14.

Department of Chemistry, Faculty of Sciences, Ataturk University, Erzurum, Turkey.

In this study, compounds with 4-hydroxybutyl, 4-phenyl, 5-carboxylate, and pyrimidine moieties were determined as α-glycosidase inhibitors. N-Substituted pyrimidinethione and acetophenone derivatives (A1-A5, B1-B11, and C1-C11) were good inhibitors of the α-glycosidase enzyme, with K values in the range of 104.27 ± 15.75 to 1,004.25 ± 100.43 nM. Among them, compound B7 was recorded as the best inhibitor, with a K of 104.27 ± 15.75 nM against α-glycosidase. In silico studies were carried out to clarify the binding affinity and interaction mode of the compounds with the best inhibition score against α-glycosidase from Saccharomyces cerevisiae. Compounds B7 (S) and B11 (R) exhibited a good binding affinity with docking scores of -8.608 and 8.582 kcal/mol, respectively. The docking results also showed that the 4-hydroxybutyl and pyrimidinethione moieties play a key role in S. cerevisiae and human α-glycosidase inhibition.
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http://dx.doi.org/10.1002/ardp.202000075DOI Listing
September 2020

Synthesis, bioactivity and binding energy calculations of novel 3-ethoxysalicylaldehyde based thiosemicarbazone derivatives.

Bioorg Chem 2020 07 12;100:103924. Epub 2020 May 12.

Institute of Marine Biotechnology, Universiti Malaysia Terengganu, 21030 Kuala Nerus, Terengganu, Malaysia.

In recent decade, the entrance of α-N-heterocyclic thiosemicarbazones derivates (Triapne, COTI-2 and DpC) in clinical trials for cancer and HIV-1 has vastly increased the interests of medicinal chemists towards this class of organic compounds. In the given study, a series of eighteen new (3a-r) 3-ethoxy salicylaldehyde-based thiosemicarbazones (TSC), bearing aryl and cycloalkyl substituents, were synthesized and assayed for their pharmacological potential against carbonic anhydrases (hCA I and hCA II), cholinesterases (AChE and BChE) and α-glycosidase. The hCA I isoform was inhibited by these novel 3-ethoxysalicylaldehyde thiosemicarbazone derivatives (3a-r) in low nanomolar levels, the Ki of which differed between 144.18 ± 26.74 and 454.92 ± 48.32 nM. Against the physiologically dominant isoform hCA II, the novel compounds demonstrated Ks varying from 110.54 ± 14.05 to 444.12 ± 36.08 nM. Also, these novel derivatives (3a-r) effectively inhibited AChE, with Ki values in the range of 385.38 ± 45.03 to 983.04 ± 104.64 nM. For BChE was obtained with Ki values in the range of 400.21 ± 35.68 to 1003.02 ± 154.27 nM. For α-glycosidase the most effective Ki values of 3l, 3n, and 3q were with Ki values of 12.85 ± 1.05, 16.03 ± 2.84, and 19.16 ± 2.66 nM, respectively. Moreover, the synthesized TCSs were simulated using force field methods whereas the binding energies of the selected compounds were estimated using MM-GBSA method. The findings indicate the present novel 3-ethoxy salicylaldehyde-based thiosemicarbazones to be excellent hits for pharmaceutical applications.
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http://dx.doi.org/10.1016/j.bioorg.2020.103924DOI Listing
July 2020

The biological activities, molecular docking studies, and anticancer effects of 1-arylsuphonylpyrazole derivatives.

J Biomol Struct Dyn 2021 Jun 15;39(9):3336-3346. Epub 2020 May 15.

Faculty of Sciences, Department of Chemistry, Ataturk University, Erzurum, Turkey.

This work is devoted to definition of the direction of reaction between 1-benzenesulfonylimino pyridinium chloride and α- or β-halo-containing sulfamides, chloroacetic acid, 1-chloro-2,3-dihydroxypropane, etc. The optimal conditions for the synchronous reaction of heterocyclization are determined. Benzenesulfonyliminopyridinium chloride was obtained to form pyrazolopyridines with 1,2-polarophiles, and pyridazine pyridines with 1,3-polarophiles. These novel derivatives were found as effective inhibitors of the α-glycosidase with K values in the range of 13.66 ± 2.63-60.63 ± 12.71 nM. The molecules () against enzyme were compared theoretically with the help of molecular docking to compare biological activities. The results were compared with the numerical values of the parameters obtained from molecular docking calculations and found to be in great agreement with the experimental results. However, ADME analysis of molecules was performed. Also, the compounds exhibited significant anticancer effect depending on the doses administered.Communicated by Ramaswamy H. Sarma.
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http://dx.doi.org/10.1080/07391102.2020.1763838DOI Listing
June 2021

Novel functionally substituted esters based on sodium diethyldithiocarbamate derivatives: Synthesis, characterization, biological activity and molecular docking studies.

Bioorg Chem 2020 06 14;99:103762. Epub 2020 Mar 14.

Department of Chemistry, Faculty of Science, Ataturk University, 25240 Erzurum, Turkey.

Alkylation of sodium diethyldithiocarbamate with allyl-2-chloroacetate, allyl-3-chloropropionate, chloromethyl-2-(tetrahydrofuran-2-yl)acetate, and 4-(chloromethyl)-1,3-dioxolane in the aqueous medium synthesized functionally substituted esters of N, N-dietyleditiocarbamic acid (M1-M4). Most active compounds were docked into the catalytic active site of the enzyme. We identified that acetate moiety for inhibition of hCA I, hCA II, and α-glycosidase and dioxolane and thiocarbamic acid moieties for inhibition of AChE and BChE enzymes are very important. The hCA I isoform was inhibited by these novel functionally substituted esters based on sodium diethyldithiocarbamate derivatives (M1-M4) in low micromolar levels, the Ki of which differed between 48.03 ± 9.77 and 188.42 ± 46.08 µM. Against the physiologically dominant isoform hCA II, the novel compounds demonstrated Ks varying from 57.33 ± 6.21 to 174.34 ± 40.72 µM. Also, these novel derivatives (M1-M4) effectively inhibited AChE, with Ki values in the range of 115.42 ± 12.44 to 243.22 ± 43.65 µM. For BChE Ki values were found in the range of 94.33 ± 9.14 to 189.45 ± 35.88 µM. For α-glycosidase the most effective Ki values of M4 and M3 were with Ki values of 32.86 ± 7.88 and 37.63 ± 4.08 µM, respectively.
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http://dx.doi.org/10.1016/j.bioorg.2020.103762DOI Listing
June 2020

Antidiabetic and antiparasitic potentials: Inhibition effects of some natural antioxidant compounds on α-glycosidase, α-amylase and human glutathione S-transferase enzymes.

Int J Biol Macromol 2018 Nov 1;119:741-746. Epub 2018 Aug 1.

Sen Research Group, Department of Biochemistry, Faculty of Arts and Science, Dumlupınar University, Evliya Çelebi Campus, 43100 Kütahya, Turkey. Electronic address:

The glutathione S-transferase (GST) was purified from fresh blood erythrocytes using affinity column chromatography. Also, α-amylase from porcine pancreas and α-glycosidase from Saccharomyces cerevisiae were used as target enzymes. In this study, these compounds were tested on α-amylase, α-glycosidase, and GST enzymes and demonstrated effective inhibitor compounds with K values in the range of 8.34-40.78 μM against GST, and 120.53-892.36 nM against α-glycosidase. Additionally, the phenolic molecules were tested for the inhibition of α-amylase enzyme which determined effective inhibition profile with IC values in the range of 175.01-626.58 nM. Indeed, these molecules can be elective inhibitors of GST, α-glycosidase and α-amylase enzymes as antidiabetic and antiparasitic agents.
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http://dx.doi.org/10.1016/j.ijbiomac.2018.08.001DOI Listing
November 2018

Novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes: Synthesis, characterization, acetylcholinesterase, butyrylcholinesterase, and carbonic anhydrase inhibitory properties.

J Biochem Mol Toxicol 2018 Sep 10;32(9):e22191. Epub 2018 Jul 10.

Department of Chemistry, Faculty of Sciences, Ataturk University, 25240, Erzurum, Turkey.

The thiolation reaction was carried out in a benzene solution at 80°C and p-substituted ketones and mercaptoacetic acid in a molar ratio (1:4) of in the presence of a catalytic amount of toluene sulfonic acids. The enzyme inhibition activities of the novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes derivatives were investigated. These novel amides of 1,1-bis-(carboxymethylthio)-1-arylethanes derivatives showed good inhibitory action against acetylcholinesterase (AChE) butyrylcholinesterase (BChE), and human carbonic anhydrase I and II isoforms (hCA I and II). AChE inhibitors, interacting with the enzyme as their primary target, are applied as relevant drugs and toxins. Many clinically established drugs are carbonic anhydrase inhibitors, and it is highly anticipated that many more will eventually find their way into the market. The novel synthesized compounds inhibited AChE and BChE with K values in the range of 0.64-1.47 nM and 9.11-48.12 nM, respectively. On the other hand, hCA I and II were effectively inhibited by these compounds, with K values between 63.27-132.34 and of 29.63-127.31 nM, respectively.
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http://dx.doi.org/10.1002/jbt.22191DOI Listing
September 2018

A hierarchical assembly of flower-like hybrid Turkish black radish peroxidase-Cu nanobiocatalyst and its effective use in dye decolorization.

Chemosphere 2017 Sep 2;182:122-128. Epub 2017 May 2.

Department of Chemistry, Faculty of Science, Erciyes University, Kayseri, 38039, Turkey. Electronic address:

Effective dye decolorization in wastewater still shows a big challenge. Although the biological methods, especially using enzymes, offer alternative and effective process for dye degradation and overcome the limitations of chemical and physical methods such as the instability, lack of reusability and high cost of free enzymes strictly, which limit their use in many scientific and technical applications. Enzymes rapidly lose their activities in aqueous solutions and against environmental changes due to their very susceptibility and unfavorable conformations. Herein, we report preparation of the enzyme-inorganic hybrid nanostructures with flower-like shape consisting of Turkish black radish peroxidase and Cu metal ions using an encouraging enzyme immobilization approach. The peroxidase-Cu hybrid nanoflowers (NFs) exhibited enhanced stability and activity towards various pH values and provided excellent dye decolorization efficiency for Victoria blue (VB) dye with more than 90% within 1 h. The NFs were also repeatedly used in efficient and caused 77% VB decolorization efficiency even at tenth cycles. However, to the best of our knowledge, for the first time, we prepared peroxidase enzyme isolated from Turkish black radish incorporated NFs and used them for dye decolorization. We believe that the NFs can be promising materials for dye decolorization in real wastewater treatment.
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http://dx.doi.org/10.1016/j.chemosphere.2017.05.012DOI Listing
September 2017

Synthesis and bioactivity of several new hetaryl sulfonamides.

J Enzyme Inhib Med Chem 2017 Dec;32(1):137-145

b Laboratory of Theoretical Bases of Synthesis and Action Mechanism of Additives , Institute of Chemistry of Additives, Azerbaijan National Academy of Sciences , Baku , Azerbaijan.

1-(4-Methylsulfonyl)-2-thione-4-aryl-5-Z-6-methyl and oxyalkyl-imidazoles were synthesized from different tetrahydropyrimidinethiones and aryl sulfonyl chloride. These compunds were tested for metal chelating effects and to determine the phrase in which inhibition occured between two physiologically pertinent compunds and carbonic anhydrase (CA) isozymes I and II (hCA I and II), butyrylcholinesterase (BChE) and acetylcholinesterase (AChE). AChE was detected in high concentrations in the brain and red blood cells. BChE is another enzymes that is abundant available in the liver and released into the blood in a soluble form. Newly synthesized hetaryl sulfonamides exhibited impressive inhibition profiles with Ki values in the range of 1.42-6.58 nM against hCA I, 1.72-7.41 nM against hCA II, 0.20-1.14 nM against AChE and 1.55-5.92 nM against BChE. Moreover, acetazolamide showed Ki values of 43.69 ± 6.44 nM against hCA I and 31.67 ± 8.39 nM against hCA II. Additionally, tacrine showed Ki values of 25.75 ± 3.39 nM and 37.82 ± 2.08 against AChE and BChE, respectively.
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http://dx.doi.org/10.1080/14756366.2016.1238367DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6009868PMC
December 2017

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

Int J Mol Sci 2016 Oct 20;17(10). Epub 2016 Oct 20.

Department of Chemistry, Faculty of Science, Atatürk University, Erzurum 25240, Turkey.

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 values of β-lactams (-) 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 (-) inhibit both carbonic anhydrases (CA) isoenzymes and AChE at low nanomolar concentrations.
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http://dx.doi.org/10.3390/ijms17101736DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5085765PMC
October 2016