دوره 22، شماره 6 - ( بهمن و اسفند 1398 )
جلد 22 شماره 6 صفحات 169-136 |
برگشت به فهرست نسخه ها
1- گروه بیوفیزیک، دانشگاه آزاد اسلامی، واحد علوم و تحقیقات، تهران، ایران.
2- گروه بیوتکنولوژی، دانشکده علوم و فناوری پیشرفته، دانشکده علوم پزشکی، دانشگاه آزاد اسلامی، تهران، ایران
3- گروه بیوفیزیک، موسسه بیوشیمی و بیوفیزیک (IBB)، دانشگاه تهران، تهران. ،goliaei@ibb.ut.ac.ir
2- گروه بیوتکنولوژی، دانشکده علوم و فناوری پیشرفته، دانشکده علوم پزشکی، دانشگاه آزاد اسلامی، تهران، ایران
3- گروه بیوفیزیک، موسسه بیوشیمی و بیوفیزیک (IBB)، دانشگاه تهران، تهران. ،
چکیده: (3082 مشاهده)
Background and Aim : Human serum albumin (HSA) is one of the richest proteins in the vascular system that regulates transport and many chemical and molecular compounds. The aim of this study was to evaluate the effect of three groups of pesticides; Insecticides, fungicides and herbicides are based on changing the molecular structure of HSA.
Materials and Methods: This systematic review covers 35 biophysical scientific-research studies related to the effect of pesticides on the structure of human serum albumin. These articles were selected through databases such as PabMed, Scopus, WebScience, Science Direct, and the Google Scholar search engine. The estimated time period was 1980 to 2019.
Ethical considerations: In this study, all the principles of ethics in research have been observed.
findings:Due to the close relationship between the biological activities of the HSA protein and its secondary structure, most articles have analyzed the secondary structure of the protein by various biophysical methods such as Fourier transform-infrared conversion, cyclic perspective and computational analysis. In general, it can be said that the pesticide-HSA interaction reduces the alpha-helix structure and increases other structures such as beta-sheet, beta-train and random coil. Most reports confirm that pesticides interact with HSA through hydrophobic, electrostatic, and hydrogen bond interactions. These interactions take place in subdomain IIA (Site One). The binding constant of pesticides to HSA protein was obtained in the range of 1-M103 to 106.
Conclusion:Pesticide-protein interactions cause changes around the only major tryptophan of the ASH protein (Trp-214), alter IIA subdomain deformation, loss of normal structure, and decrease in free HSA concentrations, resulting in impaired transport of essential compounds such as drugs and vascular hormones. Creates.
Materials and Methods: This systematic review covers 35 biophysical scientific-research studies related to the effect of pesticides on the structure of human serum albumin. These articles were selected through databases such as PabMed, Scopus, WebScience, Science Direct, and the Google Scholar search engine. The estimated time period was 1980 to 2019.
Ethical considerations: In this study, all the principles of ethics in research have been observed.
findings:Due to the close relationship between the biological activities of the HSA protein and its secondary structure, most articles have analyzed the secondary structure of the protein by various biophysical methods such as Fourier transform-infrared conversion, cyclic perspective and computational analysis. In general, it can be said that the pesticide-HSA interaction reduces the alpha-helix structure and increases other structures such as beta-sheet, beta-train and random coil. Most reports confirm that pesticides interact with HSA through hydrophobic, electrostatic, and hydrogen bond interactions. These interactions take place in subdomain IIA (Site One). The binding constant of pesticides to HSA protein was obtained in the range of 1-M103 to 106.
Conclusion:Pesticide-protein interactions cause changes around the only major tryptophan of the ASH protein (Trp-214), alter IIA subdomain deformation, loss of normal structure, and decrease in free HSA concentrations, resulting in impaired transport of essential compounds such as drugs and vascular hormones. Creates.
واژه‌های کلیدی: آلبومین سرم انسانی(HSA)، آفت‌کش‌ها، تعامل الکترواستاتیک، تعامل هیدروفوبیک، تبدیل فوریه ـ مادون قرمز، دورنگ‌نمایی دورانی
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