Issue 15, 2009

Polyelectrolyte–protein complexation driven by charge regulation

Abstract

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 α-lactalbumin, β-lactoglobulin, insulin, k-casein, lysozyme and pectin methylesterase illustrate the importance of the charge regulation mechanism. Special attention is given to pH ≅ 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.

Graphical abstract: Polyelectrolyte–protein complexation driven by charge regulation

Article information

Article type
Paper
Submitted
30 Jan 2009
Accepted
13 May 2009
First published
15 Jun 2009

Soft Matter, 2009,5, 2862-2868

Polyelectrolyte–protein complexation driven by charge regulation

F. L. B. da Silva and B. Jönsson, Soft Matter, 2009, 5, 2862 DOI: 10.1039/B902039J

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