Lattice model calculations of interactions between proteins and surface grafted polymers with tethered affinity ligands
(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:
https://lup.lub.lu.se/record/125026
- author
- Karlström, Gunnar LU and Johansson, Hans-Olof LU
- organization
- publishing date
- 2001
- 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
- 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), Biochemistry and Structural Biology (S) (000006142)
- id
- bd005346-cff8-4cc4-9a94-84c2304b7a0a (old id 125026)
- date added to LUP
- 2016-04-01 16:58:40
- date last changed
- 2023-01-05 04:15:49
@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}},
keywords = {{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}},
doi = {{10.1016/S0927-7765(00)00199-5}},
volume = {{20}},
year = {{2001}},
}