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Lysozyme adsorption to charged surfaces. A Monte Carlo study

Carlsson, F; Hyltner, E; Arnebrant, T; Malmsten, M and Linse, Per LU (2004) In The Journal of Physical Chemistry Part B 108(28). p.9871-9881
Abstract
Lysozyme adsorption to charged surfaces was studied by Monte Carlo simulations at different protein concentrations, protein net charges, ionic strengths, and surface charge densities. The lysozyme was represented by a hard sphere with embedded positive and negative surface charges parametrically dependent on the solution pH. A short-range attractive protein-protein potential was included to represent attractive non-Coulomb forces. The charged surface was described by a hard wall with embedded charges representing a mica surface. The protein adsorption was favored by high protein concentration, high protein net charge, low ionic strength, and high surface charge density. Nevertheless, adsorption appeared also for a weakly negatively charged... (More)
Lysozyme adsorption to charged surfaces was studied by Monte Carlo simulations at different protein concentrations, protein net charges, ionic strengths, and surface charge densities. The lysozyme was represented by a hard sphere with embedded positive and negative surface charges parametrically dependent on the solution pH. A short-range attractive protein-protein potential was included to represent attractive non-Coulomb forces. The charged surface was described by a hard wall with embedded charges representing a mica surface. The protein adsorption was favored by high protein concentration, high protein net charge, low ionic strength, and high surface charge density. Nevertheless, adsorption appeared also for a weakly negatively charged protein to the negatively charged surface as a result of an electrostatically favorable protein orientation at the surface. While a multipole expansion including monopole and dipole moments only was insufficient to explain preferential orientation, an expansion including also quadrupole moments provided a satisfactory picture. Finally, it was found that the short-range attraction between the proteins increased the adsorbed amount, as well as the structure in the adsorbed protein layer. The adsorbed amounts obtained compared favorably with experimental results. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Journal of Physical Chemistry Part B
volume
108
issue
28
pages
9871 - 9881
publisher
The American Chemical Society
external identifiers
  • wos:000222639900047
  • scopus:3442898466
ISSN
1520-5207
DOI
10.1021/jp0495186
language
English
LU publication?
yes
id
b4aee67a-e23a-460d-a76d-e5ddcc13be85 (old id 153978)
date added to LUP
2007-07-11 08:55:02
date last changed
2017-11-05 04:23:11
@article{b4aee67a-e23a-460d-a76d-e5ddcc13be85,
  abstract     = {Lysozyme adsorption to charged surfaces was studied by Monte Carlo simulations at different protein concentrations, protein net charges, ionic strengths, and surface charge densities. The lysozyme was represented by a hard sphere with embedded positive and negative surface charges parametrically dependent on the solution pH. A short-range attractive protein-protein potential was included to represent attractive non-Coulomb forces. The charged surface was described by a hard wall with embedded charges representing a mica surface. The protein adsorption was favored by high protein concentration, high protein net charge, low ionic strength, and high surface charge density. Nevertheless, adsorption appeared also for a weakly negatively charged protein to the negatively charged surface as a result of an electrostatically favorable protein orientation at the surface. While a multipole expansion including monopole and dipole moments only was insufficient to explain preferential orientation, an expansion including also quadrupole moments provided a satisfactory picture. Finally, it was found that the short-range attraction between the proteins increased the adsorbed amount, as well as the structure in the adsorbed protein layer. The adsorbed amounts obtained compared favorably with experimental results.},
  author       = {Carlsson, F and Hyltner, E and Arnebrant, T and Malmsten, M and Linse, Per},
  issn         = {1520-5207},
  language     = {eng},
  number       = {28},
  pages        = {9871--9881},
  publisher    = {The American Chemical Society},
  series       = {The Journal of Physical Chemistry Part B},
  title        = {Lysozyme adsorption to charged surfaces. A Monte Carlo study},
  url          = {http://dx.doi.org/10.1021/jp0495186},
  volume       = {108},
  year         = {2004},
}