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Lattice model calculations of interactions between proteins and surface grafted polymers with tethered affinity ligands

Karlström, Gunnar LU and Johansson, Hans-Olof LU (2001) In Colloids and Surfaces B: Biointerfaces 20(3). p.245-256
Abstract
Monte Carlo calculations of protein binding to affinity ligands tethered to a surface by polymers have been done and analyzed with statistical mechanical perturbation theory. The interaction of the polymers with the surface, the solvent and the protein has been varied. Different solution conditions of the polymers have been investigated, varying from collapsed polymer structures on a surface to structures extending out in the solution (athermic condition) or to mushroom like structures (hydrophobic polymers grafted on hydrophilic surface). The variation in binding of model proteins of different sizes and interactions with polymers has been studied. In general, smaller proteins bind better than larger proteins. Two types of polymer... (More)
Monte Carlo calculations of protein binding to affinity ligands tethered to a surface by polymers have been done and analyzed with statistical mechanical perturbation theory. The interaction of the polymers with the surface, the solvent and the protein has been varied. Different solution conditions of the polymers have been investigated, varying from collapsed polymer structures on a surface to structures extending out in the solution (athermic condition) or to mushroom like structures (hydrophobic polymers grafted on hydrophilic surface). The variation in binding of model proteins of different sizes and interactions with polymers has been studied. In general, smaller proteins bind better than larger proteins. Two types of polymer collapses have been studied. One type is due to increased polymer-surface attraction. The second type is due to increased polymer-self attraction. In the former case the binding, as a function of degree of collapse, decreases monotonically except for small proteins with attraction to the polymer. For collapses of the second type the loss of binding goes through a maximum except for large proteins. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Surface grafted polymer, Affinity ligand, Lattice model, Protein
in
Colloids and Surfaces B: Biointerfaces
volume
20
issue
3
pages
245 - 256
publisher
Elsevier
external identifiers
  • scopus:0035140778
ISSN
1873-4367
DOI
10.1016/S0927-7765(00)00199-5
language
English
LU publication?
yes
id
bd005346-cff8-4cc4-9a94-84c2304b7a0a (old id 125026)
date added to LUP
2007-07-05 16:48:24
date last changed
2018-05-29 10:18:53
@article{bd005346-cff8-4cc4-9a94-84c2304b7a0a,
  abstract     = {Monte Carlo calculations of protein binding to affinity ligands tethered to a surface by polymers have been done and analyzed with statistical mechanical perturbation theory. The interaction of the polymers with the surface, the solvent and the protein has been varied. Different solution conditions of the polymers have been investigated, varying from collapsed polymer structures on a surface to structures extending out in the solution (athermic condition) or to mushroom like structures (hydrophobic polymers grafted on hydrophilic surface). The variation in binding of model proteins of different sizes and interactions with polymers has been studied. In general, smaller proteins bind better than larger proteins. Two types of polymer collapses have been studied. One type is due to increased polymer-surface attraction. The second type is due to increased polymer-self attraction. In the former case the binding, as a function of degree of collapse, decreases monotonically except for small proteins with attraction to the polymer. For collapses of the second type the loss of binding goes through a maximum except for large proteins.},
  author       = {Karlström, Gunnar and Johansson, Hans-Olof},
  issn         = {1873-4367},
  keyword      = {Surface grafted polymer,Affinity ligand,Lattice model,Protein},
  language     = {eng},
  number       = {3},
  pages        = {245--256},
  publisher    = {Elsevier},
  series       = {Colloids and Surfaces B: Biointerfaces},
  title        = {Lattice model calculations of interactions between proteins and surface grafted polymers with tethered affinity ligands},
  url          = {http://dx.doi.org/10.1016/S0927-7765(00)00199-5},
  volume       = {20},
  year         = {2001},
}