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Polyelectrolyte-protein complexation driven by charge regulation

Barroso da Silva, Fernando Luis and Jönsson, Bo LU (2009) In Soft Matter 5(15). p.2862-2868
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 alpha-lactalbumin,... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Soft Matter
volume
5
issue
15
pages
2862 - 2868
publisher
Royal Society of Chemistry
external identifiers
  • wos:000268183900007
  • scopus:69249089296
ISSN
1744-6848
DOI
10.1039/b902039j
language
English
LU publication?
yes
id
c37734de-d813-425e-9ab4-90f265308f7e (old id 1460864)
date added to LUP
2009-08-24 13:03:20
date last changed
2017-11-05 04:00:26
@article{c37734de-d813-425e-9ab4-90f265308f7e,
  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 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.},
  author       = {Barroso da Silva, Fernando Luis and Jönsson, Bo},
  issn         = {1744-6848},
  language     = {eng},
  number       = {15},
  pages        = {2862--2868},
  publisher    = {Royal Society of Chemistry},
  series       = {Soft Matter},
  title        = {Polyelectrolyte-protein complexation driven by charge regulation},
  url          = {http://dx.doi.org/10.1039/b902039j},
  volume       = {5},
  year         = {2009},
}