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Volume 22, Issue 6 (February & March 2020)                   J Arak Uni Med Sci 2020, 22(6): 136-169 | Back to browse issues page

DOI: 10.32598/JAMS.22.6


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1- Department of Biophysics, Islamic Azad University, Science and Research Branch, Tehran, Iran.
2- Department of Biotechnology, Faculty of Advanced Science and Technology, Faculty of Medical Sciences, Islamic Azad University, Tehran, Iran.
3- Department of Biophysics, Institute of Biochemistry and Biophysics (IBB), University of Tehran, Iran , goliaei@ibb.ut.ac.ir
Abstract:   (552 Views)
Background and Aim: Human Serum Albumin (HSA) is one of the most abundant proteins in the blood vascular system which regulates the transportation of many chemical compounds and molecules. The purpose of this study is to review the studies about the effects of three groups of pesticides (Insecticides, herbicides and fungicides) on the molecular structure of HSA protein. 
Methods & Materials: This systematic review covers 35 studies of biophysical studies of the effect of pesticides on HSA protein. These papers were searched in PubMed, Science Direct, Web of Science databases and using Google Scholar search engine among those published from 1980 to 2019. 
Ethical Considerations: In this study, all ethical principles were considered.
Results: Given the close relationship between biological activities of HSA and its secondary structure, the most of the reviewed articles analyzed the secondary structures of the HSA using various biophysical methods such as Fourier Transform Infrared (FTIR), Circular Dichroism (CD) and computational analysis. In general, HSA-pesticides interactions can cause a reduction in α-helix structure and an increase in other secondary structures including β-sheet, β-anti, and random coils. In the most reports, it has been proven that the pesticides interact with HSA through hydrophobic and electrostatic interactions and hydrogen bonding. These interactions take place in the IIA subdomain (Site 1) of HSA. The binding constants of these interactions were in the range of 10 3 to 10 6 M-1.
Conclusion: The changes around the single important tryptophan residue of HSA (Trp-214) induce conformational deformity in the IIA subdomain of this protein which causes the loss of its native structure and leads to a decrease in free HSA concentrations which subsequently interrupt the transport of the essential compounds like drugs and hormones in the blood vascular system.
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Type of Study: Review Article | Subject: Basic Sciences
Received: 2019/05/19 | Accepted: 2019/08/4