Forces between Hydrophilic Surfaces Adsorbed with Apolipoprotein AII Alpha Helices.
(2008) In Langmuir 24(16). p.8568-8575- Abstract
- To provide better understanding of how a protein secondary structure affects protein-protein and protein-surface interactions, forces between amphiphilic alpha-helical proteins (human apolipoprotein AII) adsorbed on a hydrophilic surface (mica) were measured using an interferometric surface force apparatus (SFA). Forces between surfaces with adsorbed layers of this protein are mainly composed of electrostatic double layer forces at large surface distances and of steric repulsive forces at small distances. We suggest that the amphiphilicity of the alpha-helix structure facilitates the formation of protein multilayers next to the mica surfaces. We found that protein-surface interaction is stronger than protein-protein interaction, probably... (More)
- To provide better understanding of how a protein secondary structure affects protein-protein and protein-surface interactions, forces between amphiphilic alpha-helical proteins (human apolipoprotein AII) adsorbed on a hydrophilic surface (mica) were measured using an interferometric surface force apparatus (SFA). Forces between surfaces with adsorbed layers of this protein are mainly composed of electrostatic double layer forces at large surface distances and of steric repulsive forces at small distances. We suggest that the amphiphilicity of the alpha-helix structure facilitates the formation of protein multilayers next to the mica surfaces. We found that protein-surface interaction is stronger than protein-protein interaction, probably due to the high negative charge density of the mica surface and the high positive charge of the protein at our experimental conditions. Ellipsometry was used to follow the adsorption kinetics of this protein on hydrophilic silica, and we observed that the adsorption rate is not only controlled by diffusion, but rather by the protein-surface interaction. Our results for dimeric apolipoprotein AII are similar to those we have reported for the monomeric apolipoprotein CI, which has a similar secondary structure but a different peptide sequence and net charge. Therefore, the observed force curves seem to be a consequence of the particular features of the amphiphilic alpha-helices. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1180875
- author
- Ramos, S ; Campos-Terán, J ; Mas-Oliva, J ; Nylander, Tommy LU and Castillo, R
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Langmuir
- volume
- 24
- issue
- 16
- pages
- 8568 - 8575
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000258377900030
- pmid:18652418
- scopus:50849131197
- ISSN
- 0743-7463
- DOI
- 10.1021/la800348y
- language
- English
- LU publication?
- yes
- id
- e788ad35-327f-4861-acda-b3c73214a304 (old id 1180875)
- date added to LUP
- 2016-04-01 12:36:46
- date last changed
- 2022-04-21 17:49:36
@article{e788ad35-327f-4861-acda-b3c73214a304,
abstract = {{To provide better understanding of how a protein secondary structure affects protein-protein and protein-surface interactions, forces between amphiphilic alpha-helical proteins (human apolipoprotein AII) adsorbed on a hydrophilic surface (mica) were measured using an interferometric surface force apparatus (SFA). Forces between surfaces with adsorbed layers of this protein are mainly composed of electrostatic double layer forces at large surface distances and of steric repulsive forces at small distances. We suggest that the amphiphilicity of the alpha-helix structure facilitates the formation of protein multilayers next to the mica surfaces. We found that protein-surface interaction is stronger than protein-protein interaction, probably due to the high negative charge density of the mica surface and the high positive charge of the protein at our experimental conditions. Ellipsometry was used to follow the adsorption kinetics of this protein on hydrophilic silica, and we observed that the adsorption rate is not only controlled by diffusion, but rather by the protein-surface interaction. Our results for dimeric apolipoprotein AII are similar to those we have reported for the monomeric apolipoprotein CI, which has a similar secondary structure but a different peptide sequence and net charge. Therefore, the observed force curves seem to be a consequence of the particular features of the amphiphilic alpha-helices.}},
author = {{Ramos, S and Campos-Terán, J and Mas-Oliva, J and Nylander, Tommy and Castillo, R}},
issn = {{0743-7463}},
language = {{eng}},
number = {{16}},
pages = {{8568--8575}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Langmuir}},
title = {{Forces between Hydrophilic Surfaces Adsorbed with Apolipoprotein AII Alpha Helices.}},
url = {{http://dx.doi.org/10.1021/la800348y}},
doi = {{10.1021/la800348y}},
volume = {{24}},
year = {{2008}},
}