The green synthesis and molecular docking of novel N-substituted rhodanines as effective inhibitors for carbonic anhydrase and acetylcholinesterase enzymes |
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| Institution: | 1. Department of Chemistry, Faculty of Sciences and Arts, Bingol University, 12000-Bingöl, Turkey;2. Department of Biochemistry, Faculty of Veterinary Medicine, Bingol University, 12000-Bingöl, Turkey;3. Department of Molecular Biology and Genetics, Faculty of Arts and Science, Kilis 7 Aralik University, 79000-Kilis, Turkey;4. Department of Chemistry, Faculty of Sciences, Atatürk University, 25240-Erzurum, Turkey;1. Department of Chemistry, Faculty of Science, Akdeniz University, 07058 Antalya, Turkey;2. Department of Chemistry, Faculty of Science, Atatürk University, 25240 Erzurum, Turkey;3. Serik Gülsün Süleyman Sural Vocational School of Higher Education, Department of Opticianry Program, Akdeniz University, 07058 Antalya, Turkey;4. Central Research Laboratory, İzmir Katip Çelebi University, 35620 İzmir, Turkey;5. Faculty of Pharmacy, Ağrı İbrahim Çeçen University, 04100 Agrı, Turkey;1. Department of Chemistry, Faculty of Science and Art, Adiyaman University, 02040 Adıyaman, Turkey;2. Department of Chemistry, Faculty of Sciences, Ataturk University, 25240 Erzurum, Turkey;3. Agri Ibrahim Cecen University, Central Research and Application Laboratory, 04100 Agri, Turkey;4. Department of Molecular Biology and Genetics, Faculty of Arts and Science, Kilis 7 Aralik University, 79000 Kilis, Turkey;5. Advanced Technology Application and Research Center, Kilis 7 Aralik University, 79000 Kilis, Turkey;6. Department of Chemistry, Faculty of Art and Science, Inonu University, 44260 Malatya, Turkey;1. Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Kafrelsheikh University, Kafrelsheikh, Egypt;2. Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Ain Shams University, Cairo, Abbassia, P.O. Box 11566, Egypt;3. Department of NEUROFARBA, Section of Pharmaceutical and Nutraceutical Sciences, University of Florence, Polo Scientifico, Via U. Schiff 6, 50019, Sesto Fiorentino (Firenze), Italy;4. Department of NEUROFARBA, Section of Pharmaceutical and Nutraceutical Sciences, Laboratory of Molecular Modeling Cheminformatics & QSAR, University of Florence, Polo Scientifico, Via U. Schiff 6, 50019, Sesto Fiorentino (Firenze), Italy;5. Industrial Biotechnology Department, Genetic Engineering and Biotechnology Research Institute (GEBRI), Sadat City University, Egypt;6. Department of Pharmaceutical Chemistry, College of Pharmacy, King Saud University, P.O. Box 2457, Riyadh, 11451, Saudi Arabia;7. Department of Medicinal Chemistry, Faculty of Pharmacy, Mansoura University, Mansoura, 35516, Egypt;8. The Regional Center for Mycology and Biotechnology, Al-Azhar University, Cairo, Egypt;1. Pharmacognosy Department, College of Pharmacy, King Saud University, PO Box 2457, Riyadh 11451, Saudi Arabia;2. Drug Radiation Research Department, National Center for Radiation Research & Technology, Atomic Energy Authority, Cairo, Egypt;3. Università degli Studi di Firenze, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, I-50019 Sesto Fiorentino (Firenze), Italy;4. Pharmaceutical Chemistry Department, Faculty of Pharmacy, Cairo University, Kasr Al-Aini st., PO Box 11562, Cairo, Egypt;5. Università degli Studi di Firenze, Polo Scientifico, Dipartimento Neurofaba; Sezione di Scienze Farmaceutiche e Nutraceutiche, Via Ugo Schiff 6, 50019 Sesto Fiorentino (Firenze), Italy;1. Ataturk University, Faculty of Science, Department of Chemistry, Erzurum, Turkey;2. Erzurum Technical University, Faculty of Science, Department of Basic Sciences, Erzurum, Turkey;3. Agri Ibrahim Cecen University, Central Researching Laboratory, 04200 Agri, Turkey;4. Department of Zoology, College of Science, King Saud University, Riyadh, Saudi Arabia;5. Department of Biophysics, School of Medicine, Bahcesehir University, Istanbul, Turkey;6. Department of chemistry, Istanbul Technical University, Istanbul, Turkey |
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| Abstract: | Recently, inhibition effects of enzymes such as acetylcholinesterase (AChE) and carbonic anhydrase (CA) has appeared as a promising approach for pharmacological intervention in a variety of disorders such as epilepsy, Alzheimer’s disease and obesity. For this purpose, novel N-substituted rhodanine derivatives (RhAs) were synthesized by a green synthetic approach over one-pot reaction. Following synthesis the novel compounds, RhAs derivatives were tested against AChE and cytosolic carbonic anhydrase I, and II (hCAs I, and II) isoforms. As a result of this study, inhibition constant (Ki) were found in the range of 66.35 ± 8.35 to 141.92 ± 12.63 nM for AChE, 43.55 ± 14.20 to 89.44 ± 24.77 nM for hCA I, and 16.97 ± 1.42 to 64.57 ± 13.27 nM for hCA II, respectively. Binding energies were calculated with docking studies as −5.969, −5.981, and −9.121 kcal/mol for hCA I, hCA II, and AChE, respectively. |
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| Keywords: | Rhodanine Aza-ylides Acetylcholinesterase Carbonic anhydrase Enzyme inhibition Molecular docking |
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