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    Investigation of in vitro and in silico effects of some novel carbazole Schiff bases on human carbonic anhydrase isoforms I and II
    (Taylor & Francis Inc, 2022) Camadan, Yasemin; Cicek, Baki; Adem, Sevki; Calisir, Umit; Akkemik, Ebru
    Carbonic anhydrases (CAs, EC4.2.1.1) are metalloenzymes that catalyse reversible hydration reaction of carbon dioxide to bicarbonate and protons. In recent years, there has been a great interest in inhibitors/activators of carbonic anhydrase isoenzymes. Therefore, we investigated the effects of four different carbazole Schiff base derivatives, which are believed to have a potential to be used as a drug, on human carbonic anhydrase (hCA) isoenzymes I and II under in vitro conditions. The IC50 values of carbazole Schiff base derivatives were found to be in the range of 32.09-151.2 mu M for hCA isoenzyme I and 21.82-40.54 mu M for hCA isoenzyme II. Among all compounds, (E)-3-(((9-Octyl-9H-carbazole-3-yl)imino)methyl)benzene-1,2-diol (C3) had the strongest inhibitory effect on hCA isoenzyme II. It was determined that 2,3,4-trimethoxy and 4-hydroxy phenyl containing carbazole compounds have selective inhibition against hCA II isoenzyme. Docking studies were performed against hCA I and II receptors using induced-fit docking method. The compounds had affinity scores varying from -7.74 +/- 0.27 to -6.27 +/- 0.07 kcal/mol for hCA I and from -8.04 +/- 0.17 to -7.27 +/- 0.18 kcal/mol for hCA II. Communicated by Ramaswamy H. Sarma
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    Investigation of the Effects of 1,2,4-Triazole and Thiazole Ring-Containing Hybrid Molecules on Carbonic Anhydrase I and II
    (Wiley-V C H Verlag Gmbh, 2024) Camadan, Yasemin; Akkemik, Ebru; Guller, Pinar; Ceylan, Sule; Ozdemir, Hasan
    Carbonic anhydrase (CA, EC 4.2.1.1) is an enzyme that catalyzes the reversible reaction of carbon dioxide to bicarbonate and a proton under physiological conditions. Pharmaceutical research has gained importance since the design of novel compounds that inhibit CA I-II isoenzymes has a promising approach for pharmacological intervention in many diseases. Triazole derivatives have attracted attention due to their chemotherapeutic, antifungal, antiviral, antibiotic, analgesic, and antifungal activities. Therefore, in this study, the effect of 1,2,4-triazole and thiazole ring-containing compounds on human carbonic anhydrase I (hCA I) and II (hCA II) isoenzymes were investigated in vitro. For this purpose, hCA I and hCA II isoenzymes were purified by Sepharose-4B affinity column chromatography. Estimation of inhibition mechanism and drug-likeness characteristics of compounds were also determined using molecular docking simulation. The inhibitory effects of ten compounds were investigated. Activity vs. concentration graphs were prepared for each compound and IC50 values or AC50 were calculated from these graphs. It was revealed that some of the compounds exhibited selective inhibition on carbonic anhydrase isoenzymes. The studied compounds are considered to be drug candidates. 1,2,4-triazole and thiazole ring-containing hybrid molecules inhibited hCA-I isoenzyme with IC50 values between 0.135 and 0.523 mM and hCA II with IC50 values between 0.108 and 0.523 mM. Molecule 8 showed the highest inhibition potency against hCA-I while molecule 3 showed the highest inhibitory effect against hCA-II. Estimated binding energies for molecule 10 into hCA I is -9.31 kcal/mol and for molecule 2 on hCA II is -8.21 kcal/mol. image
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    Searching for New Natural Inhibitors of Acetylcholinesterase Enzyme
    (2022) Camadan, Yasemin; Akkemik, Ebru
    Acetylcholinesterase enzyme (AChE) is the enzyme that catalyzes the hydrolysis of the neurotransmitter acetylcholine to choline. Inhibitors of this enzyme (AChE-i) are used to treat Alzheimer's, a neurodegenerative disease. Due to the side effects of the drugs used, there has been an increased interest in investigating the inhibitory potentials of natural products which are presumed to have fewer side effects. For this purpose, the inhibitory effects of highland honey, chestnut honey, royal jelly and the seeds of peach, cherry, plum and apricot on human erythrocyte AChE enzyme was investigated in vitro in the present study. Extracts of the seeds and bee products were prepared in ethanol solvent. In order to determine the inhibitory effect of the extracts, the inhibition concentration (IC50) and Ki values which cause 50% inhibition of the enzyme were calculated using the Ellman method. It was found that among the natural product extracts studied, peach seed had the highest inhibition level (IC50 value 0.05708 mg/ml). IC50 values of highland honey, royal jelly, plum seed and apricot seed were determined as 0.2555 (mg/mL), 0.300 (mg/mL), 0.7049 (mg/mL) and 0.4544 (mg/mL) respectively.
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    Synthesis, characterizations of aryl-substituted dithiodibenzothioate derivatives, and investigating their anti-Alzheimer's properties
    (Taylor & Francis Inc, 2023) Calisir, Umit; Camadan, Yasemin; Cicek, Baki; Akkemik, Ebru; Eyupoglu, Volkan; Adem, Sevki
    The main objective of the present study was to synthesize potential inhibitor/activators of AChE and hCA I-II enzymes, which are thought to be directly related to Alzheimer's disease. Dithiodibenzothioate compounds were synthesized by thioesterification. Six different thiolate compounds produced were characterized by H-1-, C-13-NMR, FT-IR, LC-MS/MS methods. HOMO-LUMO calculations and electronic properties of all synthesized compounds were comprehensively illuminated with a semi-empirical molecular orbital (SEMO) package for organic and inorganic systems using Austin Model 1 (AM1)-Hamiltonian as implemented in the VAMP module of Materials Studio. In addition, the inhibition effects of these compounds for AChE and hCA I-II in vitro conditions were investigated. It was revealed that TE-1, TE-2, TE-3, TE-4, TE-5, and TE-6 compounds inhibited the AChE under in vitro conditions. TE-1 compound activated the enzyme hCA I while TE-2, TE-3 TE-4 compounds inhibited it. TE-5 and TE-6, on the other hand, did not exhibit a regular inhibition profile. Similarly, TE-1 activated the hCA II enzyme whereas TE-2, TE-3, TE-4, and TE-5 compounds inhibited it. TE-6 compound did not have a consistent inhibition profile for hCA II. Docking studies were performed with the compounds against AChE and hCA I-II receptors using induced-fit docking method. Molecular Dynamics (MD) simulations for best effective three protein-ligand couple were conducted to explore the binding affinity of the considered compounds in semi-real in-silico conditions. Along with the MD results, TE-1-based protein complexes were found more stable than TE-5. Based on these studies, TE-1 compound could be considered as a potential drug candidate for AD. Communicated by Ramaswamy H. Sarma
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    The determination of the carbonic anhydrases activators in vitro effect of mixed donor crown ethers
    (Wiley, 2018) Akkemik, Ebru; Cicek, Baki; Camadan, Yasemin; Calisir, Umit; Onbasioglu, Zekai
    Carbonic anhydrases (CAs) play an important function in various physiological and pathological processes. Therefore, many researchers work in this field in order to design and synthesize new drugs. Both inhibitors and activators of CAs, which are associated with the diagnosis and treatment of many diseases, are very important. The emergence of the use of CA activators in the treatment of Alzheimer has led many scholars to work on this issue. In this study, CA activators and inhibitors are determined. The crown ethers compounds (1, 2, 3, 6, 7, 8, and 9) were found to cause activation on enzyme activities of hCA I and II. The AC(50) values on hCA I and II of the compounds are in the range of 4.6565-374.979M. The 4 (IC50; 1.301 and 3.215M for hCA I and II) and 5 (IC50; 73.96 and 378.5M for hCA I and II) compounds were found to cause inhibition on enzyme activities of hCA I and II.