Polyelectrolyte-protein complexation driven by charge regulation
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1460864
- author
- Barroso da Silva, Fernando Luis and Jönsson, Bo LU
- organization
- publishing date
- 2009
- 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
- additional info
- 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)
- id
- c37734de-d813-425e-9ab4-90f265308f7e (old id 1460864)
- date added to LUP
- 2016-04-01 13:39:23
- date last changed
- 2023-01-03 23:57:03
@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}},
doi = {{10.1039/b902039j}},
volume = {{5}},
year = {{2009}},
}