Volume 15, Issue 60 (12-2025)
NCMBJ 2025, 15(60): 93-107 |
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Valizadeh A, Maghami P, Hassani L, Imani S. Comparison of the molecular effects of abamectin and ivermectin on structural changes in bovine serum albumin protein using spectroscopic and molecular docking methods. NCMBJ 2025; 15 (60) :93-107
URL: http://ncmbjpiau.ir/article-1-1787-en.html
URL: http://ncmbjpiau.ir/article-1-1787-en.html
Department of Biology, SR.C., Islamic Azad University, Tehran, Iran.
Abstract: (16 Views)
Aim and Background: Pesticides are among the most important environmental factors that have been widely produced and used in recent years and they have undeniable effects on the environment and human health. The newly developed pesticides known as Avermectins, which includes Abamectin and Ivermectin, are effective against parasites. In this study, we compare the molecular effects of Abamectin and Ivermectin's interaction on the structural changes of bovine serum albumin (BSA).
Materials and Methods: In this study, the interaction effects of bovine serum albumin (BSA) with two compounds, Abamectin (pesticide) and Ivermectin (antiparasitic drugs), were investigated using different methods of visible-ultraviolet spectroscopy, intrinsic fluorescence at different urea concentrations, and Fourier transform infrared spectroscopy (ATR-FTIR) along with molecular modeling and thermal accumulation studies.
Results :The results of UV-Visible spectroscopy showed that increasing the concentration of ligands (Abamectin and Ivermectin) caused a decrease in the absorption intensity at a wavelength of 280 nm (hypochromic effect), indicating the occurrence of interactions between the ligands and bovine serum albumin (BSA). The study of the changes in the binding free energy (ΔG) confirmed that these interactions are spontaneous. Fluorescence spectroscopy analysis of the urea effect revealed that the emission intensity of the protein decreased more significantly in the presence of Abamectin compared to Ivermectin, indicating a change in the polarity of the microenvironment surrounding aromatic amino acid residues such as tryptophan. The results of Fourier transform infrared spectroscopy (ATR-FTIR) also showed that the content of the secondary structure of the bovine serum albumin protein in the presence of ligands has slight changes. Abamectin's binding to BSA was more stable than Ivermectin's, as the binding energy value of Abamectin (-11.9 kcal/mol) is lower than that of Ivermectin (-11.0 kcal/mol). The protein aggregation results indicated that BSA is highly prone to aggregate in the presence of any ligand. Comparison of the molecular effects of these two ligands in the interaction with BSA showed that the structural changes of the protein in the interaction with Abamectin are greater than those of Ivermectin, which could be due to the difference in the type of functional groups and chemical structure of the ligands.
Conclusion: This study, using spectroscopic and molecular modeling techniques, showed that Abamectin has greater molecular effects than Ivermectin in changing the structure of BSA. Because of the distinctions in the type of interaction and the chemical composition and functional groups of these ligands.
Materials and Methods: In this study, the interaction effects of bovine serum albumin (BSA) with two compounds, Abamectin (pesticide) and Ivermectin (antiparasitic drugs), were investigated using different methods of visible-ultraviolet spectroscopy, intrinsic fluorescence at different urea concentrations, and Fourier transform infrared spectroscopy (ATR-FTIR) along with molecular modeling and thermal accumulation studies.
Results :The results of UV-Visible spectroscopy showed that increasing the concentration of ligands (Abamectin and Ivermectin) caused a decrease in the absorption intensity at a wavelength of 280 nm (hypochromic effect), indicating the occurrence of interactions between the ligands and bovine serum albumin (BSA). The study of the changes in the binding free energy (ΔG) confirmed that these interactions are spontaneous. Fluorescence spectroscopy analysis of the urea effect revealed that the emission intensity of the protein decreased more significantly in the presence of Abamectin compared to Ivermectin, indicating a change in the polarity of the microenvironment surrounding aromatic amino acid residues such as tryptophan. The results of Fourier transform infrared spectroscopy (ATR-FTIR) also showed that the content of the secondary structure of the bovine serum albumin protein in the presence of ligands has slight changes. Abamectin's binding to BSA was more stable than Ivermectin's, as the binding energy value of Abamectin (-11.9 kcal/mol) is lower than that of Ivermectin (-11.0 kcal/mol). The protein aggregation results indicated that BSA is highly prone to aggregate in the presence of any ligand. Comparison of the molecular effects of these two ligands in the interaction with BSA showed that the structural changes of the protein in the interaction with Abamectin are greater than those of Ivermectin, which could be due to the difference in the type of functional groups and chemical structure of the ligands.
Conclusion: This study, using spectroscopic and molecular modeling techniques, showed that Abamectin has greater molecular effects than Ivermectin in changing the structure of BSA. Because of the distinctions in the type of interaction and the chemical composition and functional groups of these ligands.
Type of Study: Research Article |
Subject:
Cellular and molecular
Received: 2025/12/20 | Accepted: 2025/12/1 | Published: 2025/12/1
Received: 2025/12/20 | Accepted: 2025/12/1 | Published: 2025/12/1
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