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A correlation of thermodynamic parameters with size of copper-chelated albumin aggregates.

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Title: A correlation of thermodynamic parameters with size of copper-chelated albumin aggregates.
Authors: Bansal, Ruby1 (AUTHOR), Pattanayek, Sudip K.1 (AUTHOR) sudip@chemical.iitd.ac.in, Bansal, Rohit1 (AUTHOR), Rathore, Anurag S.1 (AUTHOR)
Source: Colloid & Polymer Science. Dec2021, Vol. 299 Issue 12, p1945-1953. 9p.
Subjects: Gel permeation chromatography, Copper proteins, Serum albumin, Protein conformation, Metal ions, Albumins
Abstract: Protein conformations are strictly related to its biological function, and the variation in the structure has a major impact on human health. Metal ions are known to participate in the numerous severe pathological transformations that lead to protein aggregation. We explored the binding of Cu(II) ions to albumin with variation in extent of aggregation. The proportion of aggregates of albumin is varied by changing the time of thermally induced aggregation at the temperature of 65 °C. Utility of isothermal titration calorimeter (ITC) to study the interaction of aggregated protein with copper has not been explored yet. Establishing the association between the size of aggregates and thermodynamic parameters obtained on interaction between aggregated proteins with the metal ion will prove beneficial for future scientific applications of drug-protein interactions. We have determined the thermodynamic parameters of metal ion binding to aggregated bovine serum albumin. The size and aggregation of protein was investigated by using dynamic light scattering and size exclusion chromatography respectively. We have found that the electrostatic interaction between the aggregates and the Cu(II) is predominant. [ABSTRACT FROM AUTHOR]
Copyright of Colloid & Polymer Science is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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  Data: A correlation of thermodynamic parameters with size of copper-chelated albumin aggregates.
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  Data: <searchLink fieldCode="JN" term="%22Colloid+%26+Polymer+Science%22">Colloid & Polymer Science</searchLink>. Dec2021, Vol. 299 Issue 12, p1945-1953. 9p.
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  Data: <searchLink fieldCode="DE" term="%22Gel+permeation+chromatography%22">Gel permeation chromatography</searchLink><br /><searchLink fieldCode="DE" term="%22Copper+proteins%22">Copper proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Serum+albumin%22">Serum albumin</searchLink><br /><searchLink fieldCode="DE" term="%22Protein+conformation%22">Protein conformation</searchLink><br /><searchLink fieldCode="DE" term="%22Metal+ions%22">Metal ions</searchLink><br /><searchLink fieldCode="DE" term="%22Albumins%22">Albumins</searchLink>
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  Label: Abstract
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  Data: Protein conformations are strictly related to its biological function, and the variation in the structure has a major impact on human health. Metal ions are known to participate in the numerous severe pathological transformations that lead to protein aggregation. We explored the binding of Cu(II) ions to albumin with variation in extent of aggregation. The proportion of aggregates of albumin is varied by changing the time of thermally induced aggregation at the temperature of 65 °C. Utility of isothermal titration calorimeter (ITC) to study the interaction of aggregated protein with copper has not been explored yet. Establishing the association between the size of aggregates and thermodynamic parameters obtained on interaction between aggregated proteins with the metal ion will prove beneficial for future scientific applications of drug-protein interactions. We have determined the thermodynamic parameters of metal ion binding to aggregated bovine serum albumin. The size and aggregation of protein was investigated by using dynamic light scattering and size exclusion chromatography respectively. We have found that the electrostatic interaction between the aggregates and the Cu(II) is predominant. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
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  Data: <i>Copyright of Colloid & Polymer Science is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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RecordInfo BibRecord:
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      – Type: doi
        Value: 10.1007/s00396-021-04911-9
    Languages:
      – Code: eng
        Text: English
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        PageCount: 9
        StartPage: 1945
    Subjects:
      – SubjectFull: Gel permeation chromatography
        Type: general
      – SubjectFull: Copper proteins
        Type: general
      – SubjectFull: Serum albumin
        Type: general
      – SubjectFull: Protein conformation
        Type: general
      – SubjectFull: Metal ions
        Type: general
      – SubjectFull: Albumins
        Type: general
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      – TitleFull: A correlation of thermodynamic parameters with size of copper-chelated albumin aggregates.
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            NameFull: Pattanayek, Sudip K.
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            NameFull: Bansal, Rohit
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            NameFull: Rathore, Anurag S.
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            – D: 01
              M: 12
              Text: Dec2021
              Type: published
              Y: 2021
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              Value: 12
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            – TitleFull: Colloid & Polymer Science
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