Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes

Curtis, Robin; Prausnitz, John M.; Blanch, Harvey W.

doi:10.1002/(sici)1097-0290(19980105)57:1<11::aid-bit2>3.0.co;2-y

Cited by 211 publications

(129 citation statements)

References 40 publications

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“…[1][2][3][4][5][6][7][8][9][10][11][12] One way to modify these factors is by varying the concentration of additives in solution. As a result, conformational changes, 2 protein precipitation, and protein crystallization may occur.…”

Section: Introductionmentioning

confidence: 91%

The Effect of Salt Stoichiometry on Protein−Salt Interactions Determined by Ternary Diffusion in Aqueous Solutions

2006

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We report the four diffusion coefficients for the lysozyme-MgCl 2 -water ternary system at 25°C and pH 4.5. The comparison with previous results for the lysozyme-NaCl-water ternary system is used to examine the effect of salt stoichiometry on the transport properties of lysozyme-salt aqueous mixtures. We find that the two cross-diffusion coefficients are very sensitive to salt stoichiometry. One of the cross-diffusion coefficients is examined in terms of common-ion, excluded-volume, and protein-preferential hydration effects. We use the four ternary diffusion coefficients to extract chemical-potential cross-derivatives and proteinpreferential interaction coefficients. These thermodynamic data characterize the protein-salt thermodynamic interactions. We demonstrate the presence of the common-ion effect (Donnan effect) by analyzing the dependence of the preferential-interaction coefficient not only with respect to salt concentration but also with respect to salt stoichiometry. We conclude that the common-ion effect and the protein-preferential hydration are both important for describing the lysozyme-MgCl 2 thermodynamic interaction.

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Section: Introductionmentioning

confidence: 91%

The Effect of Salt Stoichiometry on Protein−Salt Interactions Determined by Ternary Diffusion in Aqueous Solutions

2006

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“…Specifically, B 22 can be expressed as (3) where W(r) is potential of mean force; k, the Boltzmann constant and r, the intermolecular center-to-center distance. Note that Eq.…”

Section: Theoretical Approachmentioning

confidence: 99%

“…Association constants are normally used for strong protein interactions that can be measured by using methods like surface plasmon resonance or fluorescence polarization. Instead, weak protein interactions are often characterized in terms of the osmotic second virial coefficient, B 22 . This is mainly because this coefficient can be measured by traditional colloidal characterization techniques, as well as newer methods such as static light scattering [8], smallangle x-ray [9], or neutron scattering [10], and membrane osmometry [11].…”

Section: Introductionmentioning

confidence: 99%

Effects of pH, salt type, and ionic strength on the second virial coefficients of aqueous bovine serum albumin solutions

Park

Choi

2009

Korean J. Chem. Eng.

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The osmotic pressures of aqueous bovine serum albumin (BSA) solutions were measured at different pH (3.6, 4.6, 5.6, and 7.6) in combination with different concentrations (0.01 M, 0.1 M, 1 M, and 3 M) of salts (sodium, pottasium, and lithum) by using a Wescor colloid membrane osmometer. The osmotic second virial coefficients for BSA were determined from the experimental osmotic pressure. Predominant forces between protein molecules were measured at the various pH, ionic strength, and type of salt. These experimental data were utilized to determine the depth of square-well potential, which accounts for specific interactions between protein molecules at various conditions.

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“…In fact, there are quite a few sets of experiments pertinent to our analysis. 14,[20][21][22][23][24][25][26][27][28] It turns out that there is appreciable scatter in the data if we plot all measurements of B 2 at a pH of about 4.5 as a function of ionic strength I ͓NaClϩsmall amount of Na acetate; we have set the ionic strength arising from the latter equal to 0.6ϫconcentration ͑Ref. 21͔͒ ͑see Fig.…”

Section: B Application To Lysozyme 1 Experimental Datamentioning

confidence: 99%

Optimized Baxter model of protein solutions: Electrostatics versus adhesion

Prinsen

Odijk

2004

The Journal of Chemical Physics

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A theory is set up of spherical proteins interacting by screened electrostatics and constant adhesion, in which the effective adhesion parameter is optimized by a variational principle for the free energy. An analytical approach to the second virial coefficient is first outlined by balancing the repulsive electrostatics against part of the bare adhesion. A theory similar in spirit is developed at nonzero concentrations by assuming an appropriate Baxter model as the reference state. The first-order term in a functional expansion of the free energy is set equal to zero which determines the effective adhesion as a function of salt and protein concentrations. The resulting theory is shown to have fairly good predictive power for the ionic-strength dependence of both the second virial coefficient and the osmotic pressure or compressibility of lysozyme up to about 0.2 volume fraction.

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Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes

Cited by 211 publications

References 40 publications

The Effect of Salt Stoichiometry on Protein−Salt Interactions Determined by Ternary Diffusion in Aqueous Solutions

The Effect of Salt Stoichiometry on Protein−Salt Interactions Determined by Ternary Diffusion in Aqueous Solutions

Effects of pH, salt type, and ionic strength on the second virial coefficients of aqueous bovine serum albumin solutions

Optimized Baxter model of protein solutions: Electrostatics versus adhesion

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