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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Main Authors: G. Rezaei Behbehani, Moayed Hossaini Sadr, H. Nabipur, L. Barzegar
Format: Article
Language:English
Published: Wiley 2013-01-01
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.
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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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