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A Thermodynamic Study on the Binding of Human Serum Albumin with New Synthesized Anti Cancer Pd (II) Complex

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Abstract

The thermodynamics of the interaction between new synthesized anti-cancer drug (2,2′-bipyridin n-butyl dithiocarbamato Pd (II), ButPd), and HSA was investigated at pH=7 by isothermal titration calorimetry. A new solvation model was used to reproduce the enthalpies of HSA interaction by ButPd within a broad range of complex concentrations. The solvation parameters attained from the new model were attributed to the structural change and biological activity of HSA. The binding parameters for the interaction of ButPd and HSA indicated that the considerable conformational changes in HSA were not observed after being bound with ButPd. It was found that HSA has three identical and cooperative binding sites for ButPd.

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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 & M. J. Bagheri

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

    A. Divsalar

Authors
  1. G. Rezaei Behbehani
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  2. A. Divsalar
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  3. A. A. Saboury
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  4. M. J. Bagheri
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Correspondence to G. Rezaei Behbehani.

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Behbehani, G.R., Divsalar, A., Saboury, A.A. et al. A Thermodynamic Study on the Binding of Human Serum Albumin with New Synthesized Anti Cancer Pd (II) Complex. J Solution Chem 37, 1785–1794 (2008). https://doi.org/10.1007/s10953-008-9322-y

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  • DOI: https://doi.org/10.1007/s10953-008-9322-y

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