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A Thermodynamic Study on the Binding of PEG-Stearic Acid Copolymer with Lysozyme

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Abstract

The thermodynamics of the interaction between a copolymer of polyethyleneglycol400-stearic acid, S400, and lysozyme was investigated at pH=7.0 and 27 °C in phosphate buffer by isothermal titration calorimetry, ITC. The extended solvation model was used to reproduce the enthalpies of the S400 + lysozyme interactions. The solvation parameters recovered from the extended solvation model are attributed to the structural change of lysozyme and its biological activity. The binding parameters found for the interaction of S400 with lysozyme indicate that at low concentrations of S400, the lysozyme structure was destabilized but at higher concentrations of S400 lysozyme it was stabilized by S400. It is suggested that S400 interacts with a set of three identical binding sites on lysozyme.

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Authors and Affiliations

  1. Chemistry Department, Imam Khomeini International University, Qazvin, Iran

    G. Rezaei Behbehani

  2. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

    A. Divsalar, A. A. Saboury & A. Hekmat

  3. Department of Biological Sciences, Tarbiat Moallem University, Tehran, Iran

    A. Divsalar

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  1. G. Rezaei Behbehani
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Correspondence to G. Rezaei Behbehani.

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Rezaei Behbehani, G., Divsalar, A., Saboury, A.A. et al. A Thermodynamic Study on the Binding of PEG-Stearic Acid Copolymer with Lysozyme. J Solution Chem 38, 219–229 (2009). https://doi.org/10.1007/s10953-008-9360-5

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  • DOI: https://doi.org/10.1007/s10953-008-9360-5

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