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Original Research Article
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
and 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:
Email:
atrabbasi@yahoo.com,
abbasi@gcu.edu.pk; Tel:
+92-42-111000010 ext 266
Received: 6 September 2013
Revised accepted: 19 March
2014
Tropical
Journal of Pharmaceutical Research, May 2014;
13(5): 739-745
http://dx.doi.org/10.4314/tjpr.v13i5.13
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 |
