Binding properties and conformational change of human growth hormone upon interaction with Fe3+

Atri, Maliheh Sadat; Saboury, Ali Akbar; Rezaei‐Tavirani, Mostafa; Sanati, Mohammad Hossein; Moosavi‐Movahedi, Ali Akbar; Sadeghi, Mehdi; Mansuri-Torshizi, H.; Khodabandeh, Mahvash

doi:10.1016/j.tca.2005.08.033

Cited by 18 publications

(4 citation statements)

References 19 publications

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“…[6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23] One area of current interest is the determination of binding constants of metals (e.g., Ca(II), Cu(II) and Fe(III)) to biological macromolecules. 10,12,16,18,21,22,[24][25][26][27][28][29][30] In analyzing ITC data from such experiments, there is one important issue that has not been quantitatively addressed, but needs to be in order to obtain accurate thermodynamic parameters. Specifically, metal cations such as Cu(II) and Fe(III) are poorly soluble in aqueous solutions at physiological pH.…”

Section: Introductionmentioning

confidence: 99%

Determining Thermodynamic Parameters from Isothermal Calorimetric Isotherms of the Binding of Macromolecules to Metal Cations Originally Chelated by a Weak Ligand

et al. 2007

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An accurate data analysis method for determining stoichiometry and thermodynamic parameters from isothermal titration calorimetry data for the binding of macromolecules to metal cations that are solubilized through an association with a weak ligand is presented. This approach is applied to determine the binding constant for the association of Cu(II) to the first 16 residues of the Alzheimer's amyloid beta peptide, Abeta(1-16) under conditions where Cu(II) is rendered soluble through weak binding to glycine. At pH 7.2 and 37 degrees C, a binding constant of 1.5 x 10(9) M-1 (Kd = 0.7 nM) is determined for the association of Cu(II) with Abeta(1-16).

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Section: Introductionmentioning

confidence: 99%

Determining Thermodynamic Parameters from Isothermal Calorimetric Isotherms of the Binding of Macromolecules to Metal Cations Originally Chelated by a Weak Ligand

et al. 2007

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“…, there is no significant dimerization of hGH in solutions. 13,10 In this paper, the interaction between two different classes of minerals Mg 2+ (macro element) and Co…”

Section: +mentioning

confidence: 99%

Using the Extended Solvation theory for Thermodynamic Study on the interaction of Magnesium and Cobalt ions with human growth hormone

Behbehani¹,

Saboury²,

Divsalar³

2008

Journal of the Korean Chemical Society

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“…The calorimetric data analysis using equation (16) is a graphical fitting model, which extensively has been applied to studies on the enzyme inhibition [32][33][34]50] and metal binding to proteins [8,[58][59][60][78][79]. These two proposed data analysis for isothermal titration calorimetry is expected useful for a set of binding sites, especially for enzyme inhibition study and measurement of inhibition constant.…”

Section: Ligand Binding In One Binding Site (1:1 Stochiometry)mentioning

confidence: 99%

A review on the ligand binding studies by isothermal titration calorimetry

Saboury

2006

JICS

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Thermodynamics of biomacromolecule ligand interaction is very important to understand the structure function relationship in proteins. One of the most powerful techniques useful to obtain additional information about the structure of proteins in biophysical chemistry field is isothermal titration calorimetry (ITC). An ITC experiment is a titration of a biomacromolecule solution by a solution containing a reactant (ligand) at constant temperature to obtain the exchanged heat of the reaction. The total concentration of ligand is the independent variable under experimental control. There are many reports on data analysis for ITC to find the number of binding sites (g), the equilibrium constant (K), the Gibbs free energy of binding process (ΔG), the enthalpy of binding (ΔH) and the entropy of binding (ΔS). Moreover, ITC gives information about the type of reaction, electrostatic and hydrophobic interactions, including determination of cooperativity characterization in binding process by calculating the Hill coefficient (n). A double reciprocal plot and a graphical fitting method are two simple methods used in the enzyme inhibition and metal binding to a protein. Determination of a binding isotherm needs more ITC experiments and more complex data analysis. Protein denaturation by ligand includes two processes of binding and denaturation so that ITC data analysis are more complex. However, the enthalpy of denaturation process obtained by ITC help to understand the fine structure of a protein.

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Binding properties and conformational change of human growth hormone upon interaction with Fe3+

Cited by 18 publications

References 19 publications

Determining Thermodynamic Parameters from Isothermal Calorimetric Isotherms of the Binding of Macromolecules to Metal Cations Originally Chelated by a Weak Ligand

Determining Thermodynamic Parameters from Isothermal Calorimetric Isotherms of the Binding of Macromolecules to Metal Cations Originally Chelated by a Weak Ligand

Using the Extended Solvation theory for Thermodynamic Study on the interaction of Magnesium and Cobalt ions with human growth hormone

A review on the ligand binding studies by isothermal titration calorimetry

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