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  • Title: Protein-solid interactions: important role of solvent, ions, temperature, and buffer in protein binding to alpha-Zr(IV) phosphate.
    Author: Duff MR, Kumar CV.
    Journal: Langmuir; 2009 Nov 03; 25(21):12635-43. PubMed ID: 19856993.
    Abstract:
    The interaction of proteins with a solid surface involves a complex set of interactions, and elucidating the details of these interactions is essential in the rational design of solid surfaces for applications in biosensors, biocatalysis, and biomedical applications. We examined the enthalpy changes accompanying the binding of met-hemoglobin, met-myoglobin, and lysozyme to layered alpha-Zr(IV)phosphate (20 mM NaPipes, 1 mM TBA, pH 7.2, 298 K) by titration calorimetry, under specific conditions. The corresponding binding enthalpies for the three proteins are -24.2 +/- 2.2, -10.6 +/- 2, and 6.2 +/- 0.2 kcal/mol, respectively. The binding enthalpy depended on the charge of the protein where the binding of positively charged proteins to the negatively charged solid surface was endothermic while the binding of negatively charged proteins to the negatively charged solid was exothermic. These observations are contrary to a simple electrostatic model where binding to the oppositely charged surface is expected to be exothermic. The binding enthalpy depended on the net charge on the protein, ionic strength of the medium, the type of buffer ions present, and temperature. The temperature dependence studies of binding enthalpies resulted in the estimation of heat capacity changes accompanying the binding. The heat capacity changes observed with Hb, Mb, and lysozyme are 1.4 +/- 0.3, 0.89 +/- 0.2, and 0.74 +/- 0.1 kcal/(mol.K), respectively, and these values depended on the net charge of the protein. The enthalpy changes also depended linearly on the enthalpy of ionization of the buffer, and the numbers of protons released per protein estimated from this data are 12.6 +/- 2, 6.0 +/- 1.2, and 1.2 +/- 0.5 for Hb, Mb, and lysozyme, respectively. Binding enthalpies, independent of buffer ionization, are also estimated from these data. Entropy changes are related to the loss in the degrees of freedom when the protein binds to the solid and the displacement of solvent molecules/protons/ions from the protein-solid interface. Proton coupled protein binding is one of the major processes in these systems, which is novel, and the binding enthalpies can be predicted from the net charge of the protein, enthalpy of buffer ionization, ionic strength, and temperature.
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