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Papers by Yasemin CAMADAN
Journal of enzyme inhibition and medicinal chemistry, Jan 13, 2016
Dihydropyrimidine dehydrogenase (DPD, E.C. 1.3.1.2) was purified from sheep liver with a yield of... more Dihydropyrimidine dehydrogenase (DPD, E.C. 1.3.1.2) was purified from sheep liver with a yield of 16.7%, purification fold of 407.5 and specific activity of 0.705 EU/mg proteins. The purification procedure consisted of ammonium sulphate fractionation, DEAE ion exchange chromatography and 2',5'-ADP Sepharose-4B affinity chromatography. The molecular weight determined by SDS-PAGE and was found 111 kDa. Optimum pH, ionic strength temperature and stable pH were determined as 8.0, 0.9 mM, 50 °C and 6.0, respectively. The kinetic parameters (Km and Vmax) of the enzyme were determined with NADPH as 22.97 μM and 0.17 EU/mL, respectively. The same parameters were determined with uracil as 17.46 μM and 0.14 EU/mL, respectively. Additionally, in vitro inhibitory effects of some antidepressant drugs including escitalopram, fluoxetine, mirtazapine, haloperidol and some anaesthetic drugs including propofol and lidocaine were investigated against DPD. In addition, IC50 values for each acti...
Journal of Biochemical and Molecular Toxicology, 2018
Carbonic anhydrases (CAs) play an important function in various physiological and pathological pr... more 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 4.6565-374.979 M. The 4 (IC 50 ; 1.301 and 3.215 M for hCA I and II) and 5 (IC 50 ; 73.96 and 378.5 M for hCA I and II) compounds were found to cause inhibition on enzyme activities of hCA I and II.
Cumhuriyet Science Journal, Mar 30, 2022
Acetylcholinesterase enzyme (AChE) is the enzyme that catalyzes the hydrolysis of the neurotransm... more 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.
Journal of Biomolecular Structure and Dynamics, 2022
The main objective of the present study was to synthesize potential inhibitor/activators of AChE ... more 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 <sup>1</sup>H-, <sup>13</sup>C-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 <i>in vitro</i> 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 <i>in vitro</i> 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
Erzincan Üniversitesi Fen Bilimleri Enstitüsü Dergisi, Aug 31, 2019
Journal of enzyme inhibition and medicinal chemistry, Jan 13, 2016
Dihydropyrimidine dehydrogenase (DPD, E.C. 1.3.1.2) was purified from sheep liver with a yield of... more Dihydropyrimidine dehydrogenase (DPD, E.C. 1.3.1.2) was purified from sheep liver with a yield of 16.7%, purification fold of 407.5 and specific activity of 0.705 EU/mg proteins. The purification procedure consisted of ammonium sulphate fractionation, DEAE ion exchange chromatography and 2',5'-ADP Sepharose-4B affinity chromatography. The molecular weight determined by SDS-PAGE and was found 111 kDa. Optimum pH, ionic strength temperature and stable pH were determined as 8.0, 0.9 mM, 50 °C and 6.0, respectively. The kinetic parameters (Km and Vmax) of the enzyme were determined with NADPH as 22.97 μM and 0.17 EU/mL, respectively. The same parameters were determined with uracil as 17.46 μM and 0.14 EU/mL, respectively. Additionally, in vitro inhibitory effects of some antidepressant drugs including escitalopram, fluoxetine, mirtazapine, haloperidol and some anaesthetic drugs including propofol and lidocaine were investigated against DPD. In addition, IC50 values for each acti...
Journal of Biochemical and Molecular Toxicology, 2018
Carbonic anhydrases (CAs) play an important function in various physiological and pathological pr... more 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 4.6565-374.979 M. The 4 (IC 50 ; 1.301 and 3.215 M for hCA I and II) and 5 (IC 50 ; 73.96 and 378.5 M for hCA I and II) compounds were found to cause inhibition on enzyme activities of hCA I and II.
Cumhuriyet Science Journal, Mar 30, 2022
Acetylcholinesterase enzyme (AChE) is the enzyme that catalyzes the hydrolysis of the neurotransm... more 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.
Journal of Biomolecular Structure and Dynamics, 2022
The main objective of the present study was to synthesize potential inhibitor/activators of AChE ... more 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 <sup>1</sup>H-, <sup>13</sup>C-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 <i>in vitro</i> 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 <i>in vitro</i> 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
Erzincan Üniversitesi Fen Bilimleri Enstitüsü Dergisi, Aug 31, 2019