Enzyme Inhibition Studies of Antipyrine and Aminopyrine

Year 2019, Volume: 5 Issue: 1, 1 - 6, 27.06.2019

Nashia Stellenboom , Murat Şentürk

Abstract

The
study investigated the enzyme inhibition effects of antipyrine and aminopyrine
against two human carbonic anhydrase isoforms (hCA I and hCA II),
acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE). The
effectiveness of these compounds as possible carbonic anhydrase (CA) and
cholinesterase (ChE) inhibitors is evident from the nanomolar range IC₅₀
and K_i values obtained. The
results demonstrated that aminopyrine was a more effective inhibitor compared
with antipyrine. Moreover, molecular docking results obtained from the online
docking server SwissDock supported the inhibition activity results.

Keywords

Aminopyrine, Antipyrine, Acetylcholinesterase, Butyrylcholinesterase, Carbonic Anhydrase

References

• AUGUSTINSSON K. B. (1948), Cholinesterase: a study in comparative enzymology. Acta Physiol. Scand., 15: 1-182.
• CHENG Y, PRUSOFF W. H. (1973), Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition (IC50) of an enzymatic reaction. Biochem. Pharmacol., 22(23): 3099-3108.
• DAS N., VERMA A., SHRIVASTAVA P. K., SHRIVASTAVA S. K., (2008), Synthesis and biological evaluation of some new aryl pyrazol-3-one derivatives as potential hypoglycemic agents. Indian J. Chem., 47B: 1555-1558.
• ELLMAN, G. L., COURTNEY, K. D., ANDRES, V., FEATHERSTONE, R. M. (1961), A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol., 7: 88-95.
• GROSDIDIER A., ZOETE V., MICHIELIN. (2011), SwissDock, a protein-small molecule docking web service based on EADock DSS. Nucleic Acids Res., 39(2): W270-W277.
• GUNASEKARAN P., PERUMAL S., YOGEESWARI P., SRIRAM D. (2011), A facile four-component sequential protocol in the expedient synthesis of novel 2-aryl-5-methyl-2,3-dihydro-1H-3-pyrazolones in water and their antitubercular evaluation. Eur. J. Med. Chem., 46(9): 4530-4536.
• MARKOVIĆ V., ERIĆ S., STANOJKOVIĆ T., GLIGORIJEVIĆ N., ARANĐELOVIĆ S., TODOROVIĆ N., TRIFUNOVIĆ S., MANOJLOVIĆ N., JELIĆ R., JOKSOVIĆ M. D. (2011), Antiproliferative activity and QSAR studies of a series of new 4-aminomethylidene derivatives of some pyrazol-5-ones, Bioorg. Med. Chem. Lett., 21: 4416-4421.
• PETTERSEN E. F., GODDARD T. D., HUANG C. C., COUCH G. S., GREENBLATT D. M., MENG E. C., FERRIN T. E. (2004), UCSF Chimera – a visualization system for exploratory research and analysis, J. Comput. Chem., 25(13): 1605-1612.
• RAVAGAN R. V., VIJAYAKUMAR V., KUMARI N. S. (2009), Synthesis of some novel bioactive 4-oxy/thio substituted-1H-pyrazol-5(4H)-ones via efficient cross-Claisen condensation. Eur. J. Med. Chem., 44: 3852-3857.
• STEPANKOVA S, KOMERS K. (2008), Cholinesterases and Cholinesterase Inhibitors. Curr. Enzym. Inhib., 4: 160-171.
• SONI J. P., SEN D. J., MODH K. M. (2011), Structure activity relationship studies of synthesised pyrazolone derivatives of imidazole, benzimidazole and benztriazole moiety for anti-inflammatory activity. J. Appl. Pharm. Sci., 4: 115-120.
• SRIVALLI T., SATISH K., SUTHAKARAN R., (2011), Synthesis, Characterisation and Analgesic Evaluation of Some Pyrazolone Derivatives. Int. J. Inn. Pharm. Res., 2(4): 172-174.
• STELLENBOOM N. (2019), Comparison of the inhibitory potential towards carbonic anhydrase, acetylcholinesterase and butyrylcholinesterase of chalcone and chalcone epoxide. J. Biochem Mol Toxicol., 33(2): e22240.
• SUPURAN C. T. (2007), Therapeutic applications of the carbonic anhydrase inhibitors. Therapy, 4(3): 355-378.
• SUPURAN C. T. (2008), Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat. Rev. Drug Discov., 7: 168-181.
• SUPURAN C. T. (2018), Carbonic anhydrase activators. Future Med. Chem., 10(5): 561-573.
• VERPOORTE, J. A., MEHTA, S., EDSALL, J. T. (1976), Esterase Activities of Human Carbonic Anhydrases. J. Biol. Chem., 242: 4221-4229.