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Effect of surface grafted polymers on the adsorption of different model proteins

Jönsson, Malin LU and Johansson, Hans-Olof LU (2004) In Colloids and Surfaces B: Biointerfaces 37(3-4). p.71-81
Abstract
Adsorption of a model protein to a surface with end-grafted polymers was studied by Monte Carlo simulations. In the model the effect on protein adsorption in the presence of end-grafted polymers was evaluated by calculating the change in free energy between an end-grafted surface and a surface without polymers. The change in free energy was calculated using statistical mechanical perturbation theory. Apart from ordinary athermal polymer-polymer and protein-polymer interactions we also study a broad selection of systems by varying the interaction between proteins and polymers and effective polymer-solvent interactions. The interactions between the molecules span an interval from -0.5 to +0.5 kT. Consequently, general features of protein... (More)
Adsorption of a model protein to a surface with end-grafted polymers was studied by Monte Carlo simulations. In the model the effect on protein adsorption in the presence of end-grafted polymers was evaluated by calculating the change in free energy between an end-grafted surface and a surface without polymers. The change in free energy was calculated using statistical mechanical perturbation theory. Apart from ordinary athermal polymer-polymer and protein-polymer interactions we also study a broad selection of systems by varying the interaction between proteins and polymers and effective polymer-solvent interactions. The interactions between the molecules span an interval from -0.5 to +0.5 kT. Consequently, general features of protein adsorption to end-grafted surfaces is investigated by systematically changing properties like hydrophilicity/hydrophobicity of the polymer, protein and surface as well as grafting density, degree of polymerization and protein size. Increasing grafting density as well as degree of polymerization decreases the adsorption of protein except in systems with attractive polymer-protein interactions, where adsorption increases with increasing chain length and higher grafting density. At a critical polymer-protein interaction neither chain length nor grafting density affects the free energy of adsorption. Hydrophilic polymers were found to prevent adsorption better than hydrophobic polymers. Very small particles with radii comparable to the size of a polymer segment were, however. better excluded from the surface when using hydrophobic than hydrophilic polymers. For systems with attractive polymer-protein interaction not only the volume of the protein was shown to be of importance but also the size of the exposed surface. (C) 2004 Elsevier B.V. All rights reserved. (Less)
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author
organization
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type
Contribution to journal
publication status
published
subject
in
Colloids and Surfaces B: Biointerfaces
volume
37
issue
3-4
pages
71 - 81
publisher
Elsevier
external identifiers
  • pmid:15342016
  • wos:000224020300001
  • scopus:4444297143
ISSN
1873-4367
DOI
10.1016/j.colsurfb.2004.06.010
language
English
LU publication?
yes
id
761b88bf-7803-4e1f-b829-8112ff694f71 (old id 138711)
date added to LUP
2007-07-05 16:21:29
date last changed
2017-12-10 04:31:00
@article{761b88bf-7803-4e1f-b829-8112ff694f71,
  abstract     = {Adsorption of a model protein to a surface with end-grafted polymers was studied by Monte Carlo simulations. In the model the effect on protein adsorption in the presence of end-grafted polymers was evaluated by calculating the change in free energy between an end-grafted surface and a surface without polymers. The change in free energy was calculated using statistical mechanical perturbation theory. Apart from ordinary athermal polymer-polymer and protein-polymer interactions we also study a broad selection of systems by varying the interaction between proteins and polymers and effective polymer-solvent interactions. The interactions between the molecules span an interval from -0.5 to +0.5 kT. Consequently, general features of protein adsorption to end-grafted surfaces is investigated by systematically changing properties like hydrophilicity/hydrophobicity of the polymer, protein and surface as well as grafting density, degree of polymerization and protein size. Increasing grafting density as well as degree of polymerization decreases the adsorption of protein except in systems with attractive polymer-protein interactions, where adsorption increases with increasing chain length and higher grafting density. At a critical polymer-protein interaction neither chain length nor grafting density affects the free energy of adsorption. Hydrophilic polymers were found to prevent adsorption better than hydrophobic polymers. Very small particles with radii comparable to the size of a polymer segment were, however. better excluded from the surface when using hydrophobic than hydrophilic polymers. For systems with attractive polymer-protein interaction not only the volume of the protein was shown to be of importance but also the size of the exposed surface. (C) 2004 Elsevier B.V. All rights reserved.},
  author       = {Jönsson, Malin and Johansson, Hans-Olof},
  issn         = {1873-4367},
  language     = {eng},
  number       = {3-4},
  pages        = {71--81},
  publisher    = {Elsevier},
  series       = {Colloids and Surfaces B: Biointerfaces},
  title        = {Effect of surface grafted polymers on the adsorption of different model proteins},
  url          = {http://dx.doi.org/10.1016/j.colsurfb.2004.06.010},
  volume       = {37},
  year         = {2004},
}