Thermal Study of a Newly Synthesized Cu(II) Complex Binding to Bovine β-Lactoglobulin

Thermal Study of a Newly Synthesized Cu(II) Complex Binding to Bovine β-Lactoglobulin

We have investigated the interactions between β-lactoglobulin, BLG, and new synthesized Cu(II) complex (2,2′-dibipyridine Cu(II) chloride) using isothermal titration calorimetry (ITC) methods at different temperatures of 298 and 310 K. The heats of BLG + Cu(II) interactions are reported and analyzed...

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Main Authors: Adeleh Divsalar, Lyla Barzegar, Gholamreza Rezaei Behbehani
Format: Article
Language:English
Published: Hindawi Limited 2013-01-01
Series:Journal of Chemistry
Online Access:http://dx.doi.org/10.1155/2013/453056
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spelling doaj-a89b5032897442ffbdab27196ff16d112020-11-24T22:51:20ZengHindawi LimitedJournal of Chemistry2090-90632090-90712013-01-01201310.1155/2013/453056453056Thermal Study of a Newly Synthesized Cu(II) Complex Binding to Bovine β-LactoglobulinAdeleh Divsalar0Lyla Barzegar1Gholamreza Rezaei Behbehani2Institute of Biochemistry and Biophysics, University of Tehran, Tehran, IranChemistry Department, Faculty of Science, Islamic Azad University, Takestan Branch, Takestan, IranChemistry Department, Imam Khomeini International University, Qazvin, IranWe have investigated the interactions between β-lactoglobulin, BLG, and new synthesized Cu(II) complex (2,2′-dibipyridine Cu(II) chloride) using isothermal titration calorimetry (ITC) methods at different temperatures of 298 and 310 K. The heats of BLG + Cu(II) interactions are reported and analyzed in terms of the extended solvation theory for calculation of binding and thermodynamic parameters of the interaction. The results suggested that binding of Cu(II) complex on BLG resulted in significant changes on the tertiary structure and conformation of protein via increasing of hydrophobicity and inducing partially unfolded structure in BLG which has a good agreement with the solvation parameters recovered by the extended solvation model suggesting destabilization of the protein.http://dx.doi.org/10.1155/2013/453056
collection DOAJ
language English
format Article
sources DOAJ
author Adeleh Divsalar
Lyla Barzegar
Gholamreza Rezaei Behbehani
spellingShingle Adeleh Divsalar
Lyla Barzegar
Gholamreza Rezaei Behbehani
Thermal Study of a Newly Synthesized Cu(II) Complex Binding to Bovine β-Lactoglobulin
Journal of Chemistry
author_facet Adeleh Divsalar
Lyla Barzegar
Gholamreza Rezaei Behbehani
author_sort Adeleh Divsalar
title Thermal Study of a Newly Synthesized Cu(II) Complex Binding to Bovine β-Lactoglobulin
title_short Thermal Study of a Newly Synthesized Cu(II) Complex Binding to Bovine β-Lactoglobulin
title_full Thermal Study of a Newly Synthesized Cu(II) Complex Binding to Bovine β-Lactoglobulin
title_fullStr Thermal Study of a Newly Synthesized Cu(II) Complex Binding to Bovine β-Lactoglobulin
title_full_unstemmed Thermal Study of a Newly Synthesized Cu(II) Complex Binding to Bovine β-Lactoglobulin
title_sort thermal study of a newly synthesized cu(ii) complex binding to bovine β-lactoglobulin
publisher Hindawi Limited
series Journal of Chemistry
issn 2090-9063
2090-9071
publishDate 2013-01-01
description We have investigated the interactions between β-lactoglobulin, BLG, and new synthesized Cu(II) complex (2,2′-dibipyridine Cu(II) chloride) using isothermal titration calorimetry (ITC) methods at different temperatures of 298 and 310 K. The heats of BLG + Cu(II) interactions are reported and analyzed in terms of the extended solvation theory for calculation of binding and thermodynamic parameters of the interaction. The results suggested that binding of Cu(II) complex on BLG resulted in significant changes on the tertiary structure and conformation of protein via increasing of hydrophobicity and inducing partially unfolded structure in BLG which has a good agreement with the solvation parameters recovered by the extended solvation model suggesting destabilization of the protein.
url http://dx.doi.org/10.1155/2013/453056
work_keys_str_mv AT adelehdivsalar thermalstudyofanewlysynthesizedcuiicomplexbindingtobovineblactoglobulin
AT lylabarzegar thermalstudyofanewlysynthesizedcuiicomplexbindingtobovineblactoglobulin
AT gholamrezarezaeibehbehani thermalstudyofanewlysynthesizedcuiicomplexbindingtobovineblactoglobulin
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