Abstract
The interaction between β-lactoglobulin (BLG) and a newly synthesized Cu(II) complex (2,2′-dibipyridin Cu(II) chloride) was investigated by fluorescence spectroscopy, circular dichroism (CD) and isothermal titration calorimetry (ITC) at temperatures of 27 and 37 °C. The measured heat values of the BLG–Cu(II) complex interaction are reported and analyzed in terms of our previous extended solvation theory for calculating the binding and thermodynamic parameters for the interaction. The Cu(II) complex has a strong ability to quench the intrinsic fluorescence of BLG, to change the microenvironment of tryptophan residues, and to alter the tertiary structure of the protein. Far UV–CD results showed that the complex does not induce any significant changes in the secondary structure of BLG. However, binding of the Cu(II) complex to BLG leads to a significant change in the tertiary structure of BLG, increasing its hydrophobicity and inducing a partial unfolding. This agrees well with ITC data suggesting destabilization of the protein. This finding opens up a way to predict protein destabilization caused by ligand binding, using the extended solvation theory previously proposed.
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Abbreviations
- BLG:
-
Bovine beta lactoglobulin
- CD:
-
Circular dichroism
- ΔH°:
-
Enthalpy change
- ΔS°:
-
Entropy change
- ΔG°:
-
Gibbs energy change
- ITC:
-
Isothermal titration calorimetry
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The financial support of Research Council of Kharazmi University, University of Tehran, and the Iranian National Science Foundation (INSF) are highly appreciated.
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Divsalar, A., Saboury, A.A., Haertlé, T. et al. Spectroscopic and Calorimetric Study of 2,2′-Dibipyridin Cu(II) Chloride Binding to Bovine β-Lactoglobulin. J Solution Chem 42, 705–715 (2013). https://doi.org/10.1007/s10953-013-9987-8
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DOI: https://doi.org/10.1007/s10953-013-9987-8