Tropical Journal of Pharmaceutical Research

Original Research Article | OPEN ACCESS

Sulfonamide Derivatives of 2-Amino-1-phenylethane as Suitable Cholinesterase Inhibitors

Muhammad A Abbasi¹ , Sagheer Ahmad¹, Aziz-ur-Rehman¹, Shahid Rasool¹, Khalid M Khan², Muhammad Ashraf³, Rumana Nasar³, Tayaba Ismail³

¹Department of Chemistry, Government College University, Lahore-54000; ²HEJ Research Institute of Chemistry, International Center for Chemical and Biological Sciences, University of Karachi, Karachi-75270; ³Department of Biochemistry and Biotechnology; The Islamia University of Bahawalpur, Bahawalpur-63100, Pakistan.

For correspondence:- Muhammad Abbasi Email: atrabbasi@yahoo.com Tel:+9242111000010

Received: 6 September 2013 Accepted: 19 March 2014 Published: 23 May 2014

Citation: Abbasi MA, Ahmad S, Aziz-ur-Rehman , Rasool S, Khan KM, Ashraf M, et al. Sulfonamide Derivatives of 2-Amino-1-phenylethane as Suitable Cholinesterase Inhibitors. Trop J Pharm Res 2014; 13(5):739-745 doi: 10.4314/tjpr.v13i5.13

© 2014 The authors.
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Abstract

Purpose: To evaluate the enzyme inhibition activity of N-substituted sulfamoyl derivatives of 2-amino-1-phenylethane as probable new drug candidates for the treatment of Alzheimer’s diseases.

Methods: A series of sulfamoyl derivatives, 3a-l, of 1-amino-2-phenylethane (1) were synthesized by reacting with various aryl sulfonyl chlorides, 2a-l, in the presence of aqueous Na₂CO₃ solution under definite pH control. All the synthesized molecules were screened against three enzymes, acetyl cholinesterase (AChE), butyryl cholinesterase (BChE) and lipoxygenase (LOX). The synthesized derivatives were further characterized by infra-red spectroscopy (IR), nuclear magnetic resonance (¹H-NMR) and electron ionization–mass spectrometry (EI-MS) for structure elucidation.

Results: Screening against acetyl cholinesterase (AChE), butyryl cholinesterase (BChE) and lipoxygenase (LOX) showed these molecules to be suitable inhibitors of cholinesterase enzymes, AChE and BChE, relative to eserine, the reference standard. The molecule, 3c, remained effective with 50 % inhibitory concentration (IC₅₀) value of 82.93 ± 0.15 µM (relative to eserine with IC₅₀ value of 0.04 ± 0.0001 µM) against AChE; similarly 3d was active against BChE with IC₅₀ value of 45.65 ± 0.48 µM compared to eserine with IC₅₀ value of 0.85 ± 0.00 µM. The molecule, 3f, was inactive against all the three enzymes.

Conclusion: Overall, the results indicate that these compounds are active against cholinesterase enzymes but less potent against lipoxygenase enzyme.

Keywords: 1-Amino-2-phenylethane, Aryl sulfonyl chlorides, Cholinesterase enzymes, Lipoxygenase