Affiliation:
1. Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh 202002, India
2. Department of Biochemistry, Faculty of Dentistry, Jamia Millia Islamia, New Delhi 110025, India
Abstract
Background:
Aldicarb is a carbamate pesticide commercially used in potato crop production.
Once it enters human body, it interacts with diverse proteins and other substances.
Objective:
Aldicarb is toxic to human health and it is also a cholinesterase inhibitor, which prevents
the breakdown of acetylcholine in synapse. Human alpha-2-macroglobulin (α2M), is a large
tetrameric glycoprotein of 720 kDa with antiproteinase activity, found abundantly in plasma.
Methods:
In the present study, the interaction of aldicarb with alpha-2-macroglobulin was explored
utilizing various spectroscopic techniques and molecular docking studies.
Results:
UV-vis and fluorescence spectroscopy suggests the formation of a complex between aldicarb
and α2M apparent by increased absorbance and decreased fluorescence with static quenching
mode. CD spectroscopy indicates a slight change in the structure of alpha-2-macroglobulin. Docking
studies confirm the interaction of aldicarb with Pro- 1391, Leu-1392, Lys-1393, Val-1396,
Lys- 1397, Thr-1408, Glu-1409, Val-1410, Asp-282 and Glu-281 in the receptor binding domain at
the C-terminal of the alpha 2 macroglobulin.
Discussion:
In this work, aldicarb is shown to bind with alpha 2-macroglobulin at receptor binding
domain which is the binding site for various extracellular and intracellular ligand too. Also, affecting
the functional activity of the protein may lead to further physiological consequences.
Conclusion:
It is possible that aldicarb binds and compromises antiproteinase activity of α2M and
binding properties by inducing changes in the secondary structure of the protein.
Publisher
Bentham Science Publishers Ltd.
Subject
Biochemistry,General Medicine,Structural Biology
Cited by
6 articles.
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