Lysozyme adsorption to charged surfaces. A Monte Carlo study
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/153978
- author
- Carlsson, F ; Hyltner, E ; Arnebrant, T ; Malmsten, M and Linse, Per LU
- organization
- publishing date
- 2004
- 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 (ACS)
- 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
- 2016-04-01 15:43:54
- date last changed
- 2022-01-28 06:49:25
@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 (ACS)}},
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}},
doi = {{10.1021/jp0495186}},
volume = {{108}},
year = {{2004}},
}