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Non-covalent binding analysis of sulfamethoxazole to human serum albumin: Fluorescence spectroscopy, UV–vis, FT-IR, voltammetric and molecular modeling
This study was designed to examine the interaction of sulfamethoxazole (SMZ) with human serum albumin(HSA). Spectroscopic analysis of the emission quenching at different temperatures revealed that the quenching mechanism of human serum albumin by SMZ was static mechanism. The binding constant values...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Xi'an Jiaotong University
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5762205/ https://www.ncbi.nlm.nih.gov/pubmed/29403926 http://dx.doi.org/10.1016/j.jpha.2015.01.003 |
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author | Naik, Praveen N. Nandibewoor, Sharanappa T. Chimatadar, Shivamurthi A. |
author_facet | Naik, Praveen N. Nandibewoor, Sharanappa T. Chimatadar, Shivamurthi A. |
author_sort | Naik, Praveen N. |
collection | PubMed |
description | This study was designed to examine the interaction of sulfamethoxazole (SMZ) with human serum albumin(HSA). Spectroscopic analysis of the emission quenching at different temperatures revealed that the quenching mechanism of human serum albumin by SMZ was static mechanism. The binding constant values for the SMZ–HSA system were obtained to be 22,500 L/mol at 288 K, 15,600 L/mol at 298 K, and 8500 L/mol at 308 K. The distance r between donor and acceptor was evaluated according to the theory of Föster energy transfer. The results of spectroscopic analysis and molecular modeling techniques showed that the conformation of human serum albumin had been changed in the presence of SMZ. The thermodynamic parameters, namely enthalpy change (∆H(0)) −36.0 kJ/mol, entropy change (∆S(0)) −41.3 J/mol K and free energy change (∆G(0)) −23.7 kJ/mol, were calculated by using van׳t Hoff equation. The effect of common ions on the binding of SMZ to HSA was tested. |
format | Online Article Text |
id | pubmed-5762205 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Xi'an Jiaotong University |
record_format | MEDLINE/PubMed |
spelling | pubmed-57622052018-02-05 Non-covalent binding analysis of sulfamethoxazole to human serum albumin: Fluorescence spectroscopy, UV–vis, FT-IR, voltammetric and molecular modeling Naik, Praveen N. Nandibewoor, Sharanappa T. Chimatadar, Shivamurthi A. J Pharm Anal Original Article This study was designed to examine the interaction of sulfamethoxazole (SMZ) with human serum albumin(HSA). Spectroscopic analysis of the emission quenching at different temperatures revealed that the quenching mechanism of human serum albumin by SMZ was static mechanism. The binding constant values for the SMZ–HSA system were obtained to be 22,500 L/mol at 288 K, 15,600 L/mol at 298 K, and 8500 L/mol at 308 K. The distance r between donor and acceptor was evaluated according to the theory of Föster energy transfer. The results of spectroscopic analysis and molecular modeling techniques showed that the conformation of human serum albumin had been changed in the presence of SMZ. The thermodynamic parameters, namely enthalpy change (∆H(0)) −36.0 kJ/mol, entropy change (∆S(0)) −41.3 J/mol K and free energy change (∆G(0)) −23.7 kJ/mol, were calculated by using van׳t Hoff equation. The effect of common ions on the binding of SMZ to HSA was tested. Xi'an Jiaotong University 2015-06 2015-01-21 /pmc/articles/PMC5762205/ /pubmed/29403926 http://dx.doi.org/10.1016/j.jpha.2015.01.003 Text en © 2015 Xi’an Jiaotong University. Production and hosting by Elsevier B.V. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Original Article Naik, Praveen N. Nandibewoor, Sharanappa T. Chimatadar, Shivamurthi A. Non-covalent binding analysis of sulfamethoxazole to human serum albumin: Fluorescence spectroscopy, UV–vis, FT-IR, voltammetric and molecular modeling |
title | Non-covalent binding analysis of sulfamethoxazole to human serum albumin: Fluorescence spectroscopy, UV–vis, FT-IR, voltammetric and molecular modeling |
title_full | Non-covalent binding analysis of sulfamethoxazole to human serum albumin: Fluorescence spectroscopy, UV–vis, FT-IR, voltammetric and molecular modeling |
title_fullStr | Non-covalent binding analysis of sulfamethoxazole to human serum albumin: Fluorescence spectroscopy, UV–vis, FT-IR, voltammetric and molecular modeling |
title_full_unstemmed | Non-covalent binding analysis of sulfamethoxazole to human serum albumin: Fluorescence spectroscopy, UV–vis, FT-IR, voltammetric and molecular modeling |
title_short | Non-covalent binding analysis of sulfamethoxazole to human serum albumin: Fluorescence spectroscopy, UV–vis, FT-IR, voltammetric and molecular modeling |
title_sort | non-covalent binding analysis of sulfamethoxazole to human serum albumin: fluorescence spectroscopy, uv–vis, ft-ir, voltammetric and molecular modeling |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5762205/ https://www.ncbi.nlm.nih.gov/pubmed/29403926 http://dx.doi.org/10.1016/j.jpha.2015.01.003 |
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