A New Approach for Titration Calorimetric Data Analysis on the Binding of Magnesium Ion with Myelin Basic Protein

Abstract

The interaction of the myelin basic protein (MBP) from the bovine central nervous system with divalent magnesium ion was studied by isothermal titration calorimetry at 27°C in aqueous solution. A simple rapid method for determination of the dissociation binding constants for Mg 2+ -MBP interaction was introduced using the isothermal titration calometric data. The binding isotherm for Mg 2+ -MBP interaction is easily obtained by carrying out a titration calorimetric experiment using only one set of concentrations of MBP. There are two identical independent intrinsic association constants equal to 0.021 μmol·L −1 in the first-and second-binding sites, respectively.

A novel method for thermodynamic study on binding of copper ion with Alzheimer’s amyliod β peptide

“…We have shown previously that the enthalpies of the solute-solvent (Cu 2+ + (1 16) Aβ − in this case) interactions in the aqueous solvent (Cu 2+ -water in the present case) system, can be accounted for quantitatively in terms of three factors: preferential solvation by the components of a mixed solvent, weakening or strengthening of solvent-solvent bonds by the solute and the change in the enthalpy of the solute-solvent interactions [23][24][25][26][27][28][29][30][31][32] . This treatment leads to:…”

Thermal Study of Lysozyme Binding with β-Cyclodextrin

“…We have shown previously [4][5][6][7] that the heats of the macromolecules+ligands interactions in the aqueous solvent systems can be reproduced by the following equation:…”

Thermal Study of the Nickel Ion Interaction with Myelin Basic Protein

“…The amounts of g and K d , obtained from the slope and vertical intercept plot, are 3 and 75.015 µmol/L, respectively. Dividing the q max value of -44.444 kJmol -1 by g=3, therefore, gives H ∆ =-14.815 kJmol -1 [1][2][3]. The binding parameters are reported in table 1.…”

“…Immune responses to MBP have been implicated in the pathogenesis of multiple sclerosis (MS). All sizes isoforms and charge isomers of MBP have been predicted to be ''intrinsically unstructured'', a large class of proteins which are generally extended and conformationally adaptable [2]. The differential binding of divalent metals to isolated myelin and MBP.…”