Polyelectrolyte-protein complexation driven by charge regulation

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Polyelectrolyte-protein complexation driven by charge regulation. / Barroso da Silva, Fernando Luis; Jönsson, Bo.

In: Soft Matter, Vol. 5, No. 15, 2009, p. 2862-2868.

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Barroso da Silva, Fernando Luis ; Jönsson, Bo. / Polyelectrolyte-protein complexation driven by charge regulation. In: Soft Matter. 2009 ; Vol. 5, No. 15. pp. 2862-2868.

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TY - JOUR

T1 - Polyelectrolyte-protein complexation driven by charge regulation

AU - Barroso da Silva, Fernando Luis

AU - Jönsson, Bo

N1 - The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)

PY - 2009

Y1 - 2009

N2 - The interplay between the biocolloidal characteristics (especially size and charge), pH, salt concentration and the thermal energy results in a unique collection of mesoscopic forces of importance to the molecular organization and function in biological systems. By means of Monte Carlo simulations and semi-quantitative analysis in terms of perturbation theory, we describe a general electrostatic mechanism that gives attraction at low electrolyte concentrations. This charge regulation mechanism due to titrating amino acid residues is discussed in a purely electrostatic framework. The complexation data reported here for interaction between a polyelectrolyte chain and the proteins albumin, goat and bovine alpha-lactalbumin, beta-lactoglobulin, insulin, k-casein, lysozyme and pectin methylesterase illustrate the importance of the charge regulation mechanism. Special attention is given to pH congruent to pI where ion-dipole and charge regulation interactions could overcome the repulsive ion-ion interaction. By means of protein mutations, we confirm the importance of the charge regulation mechanism, and quantify when the complexation is dominated either by charge regulation or by the ion-dipole term.

AB - The interplay between the biocolloidal characteristics (especially size and charge), pH, salt concentration and the thermal energy results in a unique collection of mesoscopic forces of importance to the molecular organization and function in biological systems. By means of Monte Carlo simulations and semi-quantitative analysis in terms of perturbation theory, we describe a general electrostatic mechanism that gives attraction at low electrolyte concentrations. This charge regulation mechanism due to titrating amino acid residues is discussed in a purely electrostatic framework. The complexation data reported here for interaction between a polyelectrolyte chain and the proteins albumin, goat and bovine alpha-lactalbumin, beta-lactoglobulin, insulin, k-casein, lysozyme and pectin methylesterase illustrate the importance of the charge regulation mechanism. Special attention is given to pH congruent to pI where ion-dipole and charge regulation interactions could overcome the repulsive ion-ion interaction. By means of protein mutations, we confirm the importance of the charge regulation mechanism, and quantify when the complexation is dominated either by charge regulation or by the ion-dipole term.

U2 - 10.1039/b902039j

DO - 10.1039/b902039j

M3 - Article

VL - 5

SP - 2862

EP - 2868

JO - Soft Matter

JF - Soft Matter

SN - 1744-6848

IS - 15

ER -