Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions

Allahyarov, Elshad; Löwen, Hartmut; Hansen, Jean‐Pierre; Louis, Ard A.

doi:10.1103/physreve.67.051404

Cited by 57 publications

(52 citation statements)

References 94 publications

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“…The maximum in turbidity due to aggregation near 10 mM is not to be confused with minima in second virial coefficients for, for example, lysozyme and apoferritin, because those nonmonotonic salt effects, observed at ionic strengths above or even much larger than 0.1 M, [44][45][46][47] are typically manifestations of very short-range interactions, such as dipole-dipole or solvation effects, and are often highly ion-specific. 48 Here, the suppression of aggregation by the addition of salt (the opposite of "salting out") is strong evidence for electrostatically induced association, as seen for -lactoglobulin at low ionic strength near its pI.…”

Section: Figure 1 Shows the Results Of Turbidimetric Titrations In Whichmentioning

confidence: 99%

Suppression of Insulin Aggregation by Heparin

et al. 2008

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The aggregation of insulin near its isoelectric point and at low ionic strength was suppressed in the presence of heparin. To understand this effect, we used turbidimetry and stopped-flow to study the pH-and ionic strength (I)-dependence of the aggregation of heparin-free insulin. The results supported the role of interprotein electrostatic interactions, contrary to the commonly held view that such forces are minimized at pH ) pI. Electrostatic modeling of insulin (DelPhi) revealed that attractive interactions arise from the marked charge anisotropy of insulin near pI. We show how screening of the interprotein attractions by added salt lead to maximum aggregation near I ) 0.01 M, corresponding to a Debye length nearly equal to the diameter of the insulin dimer, consistent with a dipole-like protein charge distribution. This analysis is also consistent with suppression of aggregation by heparin, a strong polyanion that by binding to the positive domain of one protein, inhibits its interaction with the negative domain of another.

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Section: Figure 1 Shows the Results Of Turbidimetric Titrations In Whichmentioning

confidence: 99%

Suppression of Insulin Aggregation by Heparin

et al. 2008

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“…The effect of surface charge discretization was later examined for different geometries by several groups [56,57,58,59,60,61,62].…”

Section: Discretely Charged Surfacesmentioning

confidence: 99%

Electrostatics in soft matter

Messina

2009

J. Phys.: Condens. Matter

197

216

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Abstract. Recent progress in the understanding of the effect of electrostatics in soft matter is presented. A vast amount of materials contains ions ranging from the molecular scale (e.g., electrolyte) to the meso/macroscopic one (e.g., charged colloidal particles or polyelectrolytes). Their (micro)structure and physicochemical properties are especially dictated by the famous and redoubtable long-ranged Coulomb interaction. In particular theoretical and simulational aspects, including the experimental motivations, will be discussed.

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“…The latter fulfils Newton's third law. For more technical details we refer the reader to [48,49,[53][54][55][56]. Then the distance r is varied and the force-distance curve F(r ) is gained.…”

Section: Simulations With Two Macroionsmentioning

confidence: 99%

Nonadditivity in the effective interactions of binary charged colloidal suspensions

Allahyarov

Löwen

2009

J. Phys.: Condens. Matter

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Based on primitive model computer simulations with explicit microions, we calculate the effective interactions in a binary mixture of charged colloids with species A and B for different size and charge ratios. An optimal pairwise interaction is obtained by fitting the many-body effective forces. This interaction is close to a Yukawa (or Derjaguin-Landau-Verwey-Overbeek (DLVO)) pair potential but the AB cross-interaction is different from the geometric mean of the two direct AA and BB interactions. As a function of charge asymmetry, the corresponding nonadditivity parameter is first positive, then significantly negative and is then positive again. We finally show that an inclusion of nonadditivity within an optimal effective Yukawa model gives better predictions for the fluid pair structure than DLVO theory.

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Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions

Cited by 57 publications

References 94 publications

Suppression of Insulin Aggregation by Heparin

Suppression of Insulin Aggregation by Heparin

Electrostatics in soft matter

Nonadditivity in the effective interactions of binary charged colloidal suspensions

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