Model simulations of the adsorption of statherin to solid surfaces : Effects of surface charge and hydrophobicity
(2008) In Journal of Chemical Physics 129(18).- Abstract
The structural properties of the salivary protein statherin upon adsorption have been examined using a coarse-grained model and Monte Carlo simulation. A simple model system with focus on electrostatic interactions and short-ranged attractions among the uncharged amino acids has been used. To mimic hydrophobically modified surfaces, an extra short-ranged interaction was implemented between the amino acids and the surface. It has been shown that the adsorption and the thickness of the adsorbed layer are determined by (i) the affinity for the surface, i.e., denser layer with an extrashort-ranged potential, and (ii) the distribution of the charges along the chain. If all the amino acids have a high affinity for the surface, the protein... (More)
The structural properties of the salivary protein statherin upon adsorption have been examined using a coarse-grained model and Monte Carlo simulation. A simple model system with focus on electrostatic interactions and short-ranged attractions among the uncharged amino acids has been used. To mimic hydrophobically modified surfaces, an extra short-ranged interaction was implemented between the amino acids and the surface. It has been shown that the adsorption and the thickness of the adsorbed layer are determined by (i) the affinity for the surface, i.e., denser layer with an extrashort-ranged potential, and (ii) the distribution of the charges along the chain. If all the amino acids have a high affinity for the surface, the protein adsorbs in a train conformation, if the surface is negatively charged the protein adsorbs in a tail-train conformation, whereas if the surface is positively charged the protein adsorbs in a loop conformation. The latter gives rise to a more confined adsorbed layer.
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- author
- Skepö, M. LU
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Chemical Physics
- volume
- 129
- issue
- 18
- article number
- 185101
- pages
- 12 pages
- publisher
- American Institute of Physics (AIP)
- external identifiers
-
- pmid:19045429
- scopus:56349169061
- ISSN
- 0021-9606
- DOI
- 10.1063/1.3002317
- language
- English
- LU publication?
- no
- additional info
- Funding Information: This work was supported by grants from Malmö University.
- id
- bea2988a-c55a-4138-9bb5-7a6a6ee9c938
- date added to LUP
- 2021-10-15 06:50:47
- date last changed
- 2024-03-08 20:25:34
@article{bea2988a-c55a-4138-9bb5-7a6a6ee9c938,
abstract = {{<p>The structural properties of the salivary protein statherin upon adsorption have been examined using a coarse-grained model and Monte Carlo simulation. A simple model system with focus on electrostatic interactions and short-ranged attractions among the uncharged amino acids has been used. To mimic hydrophobically modified surfaces, an extra short-ranged interaction was implemented between the amino acids and the surface. It has been shown that the adsorption and the thickness of the adsorbed layer are determined by (i) the affinity for the surface, i.e., denser layer with an extrashort-ranged potential, and (ii) the distribution of the charges along the chain. If all the amino acids have a high affinity for the surface, the protein adsorbs in a train conformation, if the surface is negatively charged the protein adsorbs in a tail-train conformation, whereas if the surface is positively charged the protein adsorbs in a loop conformation. The latter gives rise to a more confined adsorbed layer.</p>}},
author = {{Skepö, M.}},
issn = {{0021-9606}},
language = {{eng}},
number = {{18}},
publisher = {{American Institute of Physics (AIP)}},
series = {{Journal of Chemical Physics}},
title = {{Model simulations of the adsorption of statherin to solid surfaces : Effects of surface charge and hydrophobicity}},
url = {{http://dx.doi.org/10.1063/1.3002317}},
doi = {{10.1063/1.3002317}},
volume = {{129}},
year = {{2008}},
}