Synthesis of 5-methyl-2,4-dihydro-3H-1,2,4-triazole-3-one’s aryl Schiff base derivatives and investigation of carbonic anhydrase and cholinesterase (AChE, BuChE) inhibitory properties
作者： Musa Özil , Halis Türker Balaydın , Murat Şentürk
DOI: 10.1016/J.BIOORG.2019.02.045
关键词: Enzyme 、 Triazole 、 Acetylcholinesterase 、 Schiff base 、 Biochemistry 、 Carbonic anhydrase 、 Cholinesterase 、 Aryl 、 Chemistry 、 Butyrylcholinesterase
摘要: Carbonic anhydrase enzymes (EC 4.2.1.1, CAs) are metalloenzyme families that catalyze the rapid conversion of H2O and CO2 to HCO3- H+. CAs found in different tissues where they participate various significant biochemical processes such as ion transport, carbon dioxide respiration, ureagenesis, lipogenesis, bone resorption, electrolyte secretion, acid-base balance, gluconeogenesis. In processes, many therapeutic targets because their inhibitory potentials especially treatment some diseases edema, glaucoma, obesity, cancer, epilepsy, osteoporosis. Acetylcholinesterase (AChE) Butyrylcholinesterase (BuChE) inhibitors also valuable compounds for applications including Alzheimer's disease. this work, we report a fast effective synthesis 5-methyl-2,4-dihydro-3H-1,2,4-triazole-3-one's aryl Schiff base derivatives CA cholinesterases properties. Our findings showed these derivatives, with triazole ring, strong inhibitors.
sci-hub.se 参考文章(59)
Hoh-Gyu Hahn, Jung-Sup Choi, Hee Kyung Lim, Kee-In Lee, In Taek Hwang, Triazolyl phenyl disulfides: 8-Amino-7-oxononanoate synthase inhibitors as potential herbicides Pesticide Biochemistry and Physiology. ,vol. 125, pp. 78- 83 ,(2015) , 10.1016/J.PESTBP.2015.05.006
Jacob A. Verpoorte, Suchinta Mehta, John T. Edsall, Esterase Activities of Human Carbonic Anhydrases B and C Journal of Biological Chemistry. ,vol. 242, pp. 4221- 4229 ,(1967) , 10.1016/S0021-9258(18)95800-X
Elisabeth Nagaradja, Ghenia Bentabed-Ababsa, Mathieu Scalabrini, Floris Chevallier, Stéphanie Philippot, Stéphane Fontanay, Raphaël E. Duval, Yury S. Halauko, Oleg A. Ivashkevich, Vadim E. Matulis, Thierry Roisnel, Florence Mongin, Deprotometalation-iodolysis and computed CH acidity of 1,2,3- and 1,2,4-triazoles. Application to the synthesis of resveratrol analogues. Bioorganic & Medicinal Chemistry. ,vol. 23, pp. 6355- 6363 ,(2015) , 10.1016/J.BMC.2015.08.031
Deniz Ekinci, Murat Şentürk, Ömer İrfan Küfrevioğlu, Salicylic acid derivatives: synthesis, features and usage as therapeutic tools Expert Opinion on Therapeutic Patents. ,vol. 21, pp. 1831- 1841 ,(2011) , 10.1517/13543776.2011.636354
Musa Özil, Mutlu Canpolat, Solvent-free synthesis of novel phthalocyanines containing triazole derivatives under microwave irradiation Polyhedron. ,vol. 51, pp. 82- 89 ,(2013) , 10.1016/J.POLY.2012.12.016
Alessio Innocenti, Mika Hilvo, Andrea Scozzafava, Seppo Parkkila, Claudiu T. Supuran, Carbonic anhydrase inhibitors: Inhibition of the new membrane-associated isoform XV with phenols. Bioorganic & Medicinal Chemistry Letters. ,vol. 18, pp. 3593- 3596 ,(2008) , 10.1016/J.BMCL.2008.04.077
Alessio Innocenti, Daniela Vullo, Andrea Scozzafava, Claudiu T. Supuran, Carbonic anhydrase inhibitors: Interactions of phenols with the 12 catalytically active mammalian isoforms (CA I–XIV) Bioorganic & Medicinal Chemistry Letters. ,vol. 18, pp. 1583- 1587 ,(2008) , 10.1016/J.BMCL.2008.01.077
Serdar Durdagi, Murat Şentürk, Deniz Ekinci, Halis Türker Balaydın, Süleyman Göksu, Ö. İrfan Küfrevioğlu, Alessio Innocenti, Andrea Scozzafava, Claudiu T. Supuran, Kinetic and docking studies of phenol-based inhibitors of carbonic anhydrase isoforms I, II, IX and XII evidence a new binding mode within the enzyme active site. Bioorganic & Medicinal Chemistry. ,vol. 19, pp. 1381- 1389 ,(2011) , 10.1016/J.BMC.2011.01.016
Raymond M. Dawson, Reversibility of the inhibition of acetylcholinesterase by tacrine Neuroscience Letters. ,vol. 118, pp. 85- 87 ,(1990) , 10.1016/0304-3940(90)90254-7
Esra Bayram, Murat Senturk, O Irfan Kufrevioglu, Claudiu T Supuran, None, In vitro inhibition of salicylic acid derivatives on human cytosolic carbonic anhydrase isozymes I and II Bioorganic & Medicinal Chemistry. ,vol. 16, pp. 9101- 9105 ,(2008) , 10.1016/J.BMC.2008.09.028