Bulletin of the Korean Chemical Society

  • 제28권5호
  • /
  • Pages.730-736
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  • 2007
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  • 0253-2964(pISSN)
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  • 1229-5949(eISSN)
대한화학회 (Korean Chemical Society)
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Thermodynamic and Structural Studies on the Human Serum Albumin in the Presence of a Polyoxometalate

  • Ajloo, D. (Faculty of Chemistry, Damghan University of Basic Science) ;
  • Behnam, H. (Faculty of Chemistry, Damghan University of Basic Science) ;
  • Saboury, A.A. (Institute of Biochemistry and Biophysics, The University of Tehran) ;
  • Mohamadi-Zonoz, F. (Faculty of Chemistry, Damghan University of Basic Science) ;
  • Ranjbar, B. (Department of Biophysics, Faculty of Basic Science, Tarbiat Modarres University) ;
  • Moosavi-Movahedi, A.A. (Institute of Biochemistry and Biophysics, The University of Tehran) ;
  • Hasani, Z. (Department of Biophysics, Faculty of Basic Science, Tarbiat Modarres University) ;
  • Alizadeh, K. (Department of Chemistry, Faculty of Basic Science, Tarbiat Modarres University) ;
  • Gharanfoli, M. (Institute of Biochemistry and Biophysics, The University of Tehran) ;
  • Amani, M. (Institute of Biochemistry and Biophysics, The University of Tehran)
  • 발행 : 2007.05.20
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초록

The interaction of a polyoxometal (POM), K6SiW11Co(H2O)O39.10H2O (K6) as a Keggin, with human serum albumin (HSA) was studied by different methods and techniques. Binding studies show two sets of binding sites for interaction of POM to HSA. Binding analysis and isothermal calorimetery revealed that, the first set of binding site has lower number of bound ligand per mole of protein (ν), lower Hill constant (n), higher binding constant (K), more negative entropy (ΔS) and more electrostatic interaction in comparison to the second set of binding site. In addition, differential scanning calorimetery (DSC) and spectrophotometery data showed that, there are two energetic domains. The first domain is less stable (lower Tm and Cp) which corresponds to the tail segment of HSA and another with more stability is related to the head segment of HSA. Polyoxometal also decreases the stability of protein as Tm, secondary and tertiary structure as well as quenching of the fluorescence decrease. On other hand, perturbations in tertiary structure are more than secondary structure.

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