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Behbehani, G. Rezaei,Tazikeh, E.,Saboury, A.A. Korean Chemical Society 2006 Bulletin of the Korean Chemical Society Vol.27 No.2
The enthalpies of transfer, $\Delta H_t^\theta$, of urea from water to aqueous ethanol, EtOH, propan-1-ol, PrOH, and acetonitrile, MeCN, are reported and analysed in terms of the new solvation theory. The analyses show that the solvation of urea is random in the considered solvent mixtures. It is also found that urea interact more strongly with EtOH or PrOH than water.
A New Approach for Thermodynamic Study on the Binding of Human Serum Albumin with Cerium Chloride
G. Rezaei Behbehani,A. Divsalar,A. A. Saboury,F. Faridbod,M. R. Ganjali 대한화학회 2009 Bulletin of the Korean Chemical Society Vol.30 No.6
Thermodynamics of the interaction between Cerium (III) chloride, Ce3+, with Human Serum Albumin, HSA, was investigated at pH 7.0 and 27 oC in phosphate buffer by isothermal titration calorimetry. Our recently solvation model was used to reproduce the enthalpies of HSA interaction by Ce3+. The solvation parameters recovered from our new model, attributed to the structural change of HSA and its biological activity. The interaction of HSA withCe3+ showed a set of two binding sites with negative cooperativity. Ce3+ interacts with multiple sites on HSA naffecting its biochemical and biophysical properties
A Thermodynamic Study on the Binding of Cobalt Ion with Myelin Basic Protein
G. Rezaei Behbehani*,A. A. Saboury,A. Fallah Baghery 대한화학회 2008 Bulletin of the Korean Chemical Society Vol.29 No.4
The interaction of myelin basic protein (MBP) from bovine central nervous system with divalent calcium ion was studied by isothermal titration calorimetry at 27 ℃ in aqueous solution. The extended solvation model was used to reproduce the enthalpies of Co²+-MBP interaction over the whole Co²+ concentrations. The solvation parameters recovered from the solvation model were attributed to the structural change of MBP due to the metal ion interaction. It was found that there is a set of three identical and noninteracting binding sites for Co²+ ions. The association equilibrium constant is 0.015 m M-¹. The molar enthalpy of binding is DH=-14.60 kJ mol-¹.
G. Rezaei Behbehani* 대한화학회 2005 Bulletin of the Korean Chemical Society Vol.26 No.2
The enthalpies of transfer, Ht, of NaI from water to aqueous methanol, ethanol and isopropanol, iPrOH, systems are reported. These data have been analysed in terms of the new solvation theory. These data are considered in terms of the new developed solvation theory including variable (n + N), the net effect of the solute on the solvent-solvent bonding, is positive if there is a net breaking or weakening of solvent-solvent bonds. The solvation parameters recovered from the analyses indicate that the net affect of NaI on solvent structure is a breaking of solvent-solvent bonds and that NaI is preferentially solvated by water in all aqueous alcohol systems considered. (n + N) values increase with increasing in the size of the alcohol alkyl residue from methanol to iPrOH.
A Thermodynamic Study on the Binding of Cobalt Ion with Myelin Basic Protein
Behbehani, G. Rezaei,Saboury, A.A.,Baghery, A. Fallah Korean Chemical Society 2008 Bulletin of the Korean Chemical Society Vol.29 No.4
The interaction of myelin basic protein (MBP) from bovine central nervous system with divalent calcium ion was studied by isothermal titration calorimetry at 27 ${^{\circ}C}$ in aqueous solution. The extended solvation model was used to reproduce the enthalpies of $Co^{2+}$-MBP interaction over the whole $Co^{2+}$ concentrations. The solvation parameters recovered from the solvation model were attributed to the structural change of MBP due to the metal ion interaction. It was found that there is a set of three identical and noninteracting binding sites for $Co^{2+}$ ions. The association equilibrium constant is 0.015 ${\mu}M^{-1}$. The molar enthalpy of binding is $\Delta$H = −14.60 kJ $mol^{-1}$.
A New Approach for Thermodynamic Study on the Binding of Human Serum Albumin with Cerium Chloride
Rezaei Behbehani, G.,Divsalar, A.,Saboury, A.A.,Faridbod, F.,Ganjali, M.R. Korean Chemical Society 2009 Bulletin of the Korean Chemical Society Vol.30 No.6
Thermodynamics of the interaction between Cerium (III) chloride, $Ce^{3+}$, with Human Serum Albumin, HSA, was investigated at pH 7.0 and $27\;{^{\circ}C}$ in phosphate buffer by isothermal titration calorimetry. Our recently solvation model was used to reproduce the enthalpies of HSA interaction by $Ce^{3+}$. The solvation parameters recovered from our new model, attributed to the structural change of HSA and its biological activity. The interaction of HSA with $Ce^{3+}$ showed a set of two binding sites with negative cooperativity. $Ce^{3+}$ interacts with multiple sites on HSA affecting its biochemical and biophysical properties.
M. Saeidfar,H. Masouri-Torshizi,G. Rezaei Behbehani,A. Divsalar,A. A. Saboury 대한화학회 2009 Bulletin of the Korean Chemical Society Vol.30 No.9
A Thermodynamic study on the interaction of bovine calf thymus DNA with new designed Pd(II) complex (Ethylendiamine- 8-hydroxyquinolinato Palladium(II) chloride) was studied by using isothermal titration calorimetry (ITC) at 27 °C in Tris buffer solution at pH = 7.5. The enthalpies of Pd(II) complex + DNA interaction are reported and analysed in terms of the new solvation theory. It was indicated that there are three identical and non-cooperative sites for Pd(II) complex. The binding of a Pd(II) complex is endothermic with association equilibrium constants of 428.03 mM-1 at 27 °C . The binding of Pd(II) complex can cause some changes in the stability of the DNA at low and high Pd(II) complex concentrations. Our results suggested that this complex might interact with DNA as an intercalator, thus interfering with DNA replication and cell proliferation.
Saeidfar, M.,Masouri-Torshizi, H.,Behbehani, G. Rezaei,Divsalar, A.,Saboury, A.A. Korean Chemical Society 2009 Bulletin of the Korean Chemical Society Vol.30 No.9
A Thermodynamic study on the interaction of bovine calf thymus DNA with new designed Pd(II) complex (Ethylendiamine- 8-hydroxyquinolinato Palladium(II) chloride) was studied by using isothermal titration calorimetry (ITC) at 27 ${^{\circ}C}$ in Tris buffer solution at pH = 7.5. The enthalpies of Pd(II) complex + DNA interaction are reported and analysed in terms of the new solvation theory. It was indicated that there are three identical and non-cooperative sites for Pd(II) complex. The binding of a Pd(II) complex is endothermic with association equilibrium constants of 428.03 m$M^{-1}$ at 27 ${^{\circ}C}$. The binding of Pd(II) complex can cause some changes in the stability of the DNA at low and high Pd(II) complex concentrations. Our results suggested that this complex might interact with DNA as an intercalator, thus interfering with DNA replication and cell proliferation.