A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin
Binding parameters of the N-phenyl benzene sulfonyl hydrazide, sulfonamide, and nanosulfonamide interaction with human serum albumin were determined by calorimetry method. The obtained binding parameters indicated that sulfonamide in the second binding sites has higher affinity for binding than the...
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2013-01-01
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Series: | Journal of Chemistry |
Online Access: | http://dx.doi.org/10.1155/2013/120480 |
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author | G. Rezaei Behbehani Moayed Hossaini Sadr H. Nabipur L. Barzegar |
author_facet | G. Rezaei Behbehani Moayed Hossaini Sadr H. Nabipur L. Barzegar |
author_sort | G. Rezaei Behbehani |
collection | DOAJ |
description | Binding parameters of the N-phenyl benzene sulfonyl hydrazide, sulfonamide, and nanosulfonamide interaction with human serum albumin were determined by calorimetry method. The obtained binding parameters indicated that sulfonamide in the second binding sites has higher affinity for binding than the first binding sites. The binding process of sulfonamide to HSA is both enthalpy and entropy driven. The associated equilibrium constants confirm that sulfonamide binds to HSA with high affinity (2.2×106
and 3.86105 M−1 for first and second sets of binding sites, resp.). The obtained results indicate that sulfonamide increases the HSA antioxidant property. Nanosulfonamide has much more affinity for HSA (3.6×106 M−1) than sulfonamide. |
format | Article |
id | doaj-art-6e4b24e7b5f64868a3d88091005dd718 |
institution | Kabale University |
issn | 2090-9063 2090-9071 |
language | English |
publishDate | 2013-01-01 |
publisher | Wiley |
record_format | Article |
series | Journal of Chemistry |
spelling | doaj-art-6e4b24e7b5f64868a3d88091005dd7182025-02-03T07:24:43ZengWileyJournal of Chemistry2090-90632090-90712013-01-01201310.1155/2013/120480120480A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum AlbuminG. Rezaei Behbehani0Moayed Hossaini Sadr1H. Nabipur2L. Barzegar3Chemistry Department, Imam Khomeini International University, Qazvin, IranChemistry Department, Faculty of Science, Azarbaijan Shahid Madani University, Tabriz, IranChemistry Department, Faculty of Science, Azarbaijan Shahid Madani University, Tabriz, IranChemistry Department, Faculty of Science, Islamic Azad University, Takestan Branch, Takestan, IranBinding parameters of the N-phenyl benzene sulfonyl hydrazide, sulfonamide, and nanosulfonamide interaction with human serum albumin were determined by calorimetry method. The obtained binding parameters indicated that sulfonamide in the second binding sites has higher affinity for binding than the first binding sites. The binding process of sulfonamide to HSA is both enthalpy and entropy driven. The associated equilibrium constants confirm that sulfonamide binds to HSA with high affinity (2.2×106 and 3.86105 M−1 for first and second sets of binding sites, resp.). The obtained results indicate that sulfonamide increases the HSA antioxidant property. Nanosulfonamide has much more affinity for HSA (3.6×106 M−1) than sulfonamide.http://dx.doi.org/10.1155/2013/120480 |
spellingShingle | G. Rezaei Behbehani Moayed Hossaini Sadr H. Nabipur L. Barzegar A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin Journal of Chemistry |
title | A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin |
title_full | A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin |
title_fullStr | A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin |
title_full_unstemmed | A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin |
title_short | A Comparative Study on the Interaction of Sulfonamide and Nanosulfonamide with Human Serum Albumin |
title_sort | comparative study on the interaction of sulfonamide and nanosulfonamide with human serum albumin |
url | http://dx.doi.org/10.1155/2013/120480 |
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