Interaction of dissolved proteins with spherical polyelectrolyte brushes

Kurzanzeige
dc.contributor.authorWittemann, Alexander
dc.contributor.authorHaupt, Björndeu
dc.contributor.authorMerkle, R.deu
dc.contributor.authorBallauff, Matthiasdeu
dc.date.accessioned2012-08-24T07:00:09Zdeu
dc.date.available2012-08-24T07:00:09Zdeu
dc.date.issued2003
dc.description.abstractWe consider the adsorption of bovine serum albumin (BSA) on spherical polyelectrolyte brushes (SPB). The SPB consist of a solid polystyrene core of 100nm diameter onto which linear polyelectrolyte chains (poly(acrylic acid), (PAA)) are grafted. The adsorption of BSA is studied at a pH of 6.1 at different concentrations of added salt and buffer (MES). We observe strong adsorption of BSA onto the SPB despite the effect that the particles as well as the dissolved BSA are charged negatively. The adsorption of BSA is strongest at low salt concentration and decreases drastically with increasing amounts of added salt. The adsorbed protein can be washed out again by raising the ionic strength. The various driving forces for the adsorption are discussed. It is demonstrated that the main driving force is located in the electrostatic interaction of the protein with the brush layer of the particles. All data show that the SPB present a new class of carrier particles whose interaction with proteins can be tuned in a well-defined manner.eng
dc.description.versionpublished
dc.identifier.citationPubl. in: Macromolecular Symposia ; 191 (2003), 1. - pp. 81–88deu
dc.identifier.doi10.1002/masy.200390017deu
dc.identifier.urihttp://kops.uni-konstanz.de/handle/123456789/20222
dc.language.isoengdeu
dc.legacy.dateIssued2012-08-24deu
dc.rightsterms-of-usedeu
dc.rights.urihttps://rightsstatements.org/page/InC/1.0/deu
dc.subjectpolyelectrolyte brushdeu
dc.subjectproteinsdeu
dc.subjectBSAdeu
dc.subjectadsorptiondeu
dc.subject.ddc540deu
dc.titleInteraction of dissolved proteins with spherical polyelectrolyte brusheseng
dc.typeJOURNAL_ARTICLEdeu
dspace.entity.typePublication
kops.citation.bibtex
@article{Wittemann2003Inter-20222,
  year={2003},
  doi={10.1002/masy.200390017},
  title={Interaction of dissolved proteins with spherical polyelectrolyte brushes},
  number={1},
  volume={191},
  issn={1022-1360},
  journal={Macromolecular Symposia},
  pages={81--88},
  author={Wittemann, Alexander and Haupt, Björn and Merkle, R. and Ballauff, Matthias}
}
kops.citation.iso690WITTEMANN, Alexander, Björn HAUPT, R. MERKLE, Matthias BALLAUFF, 2003. Interaction of dissolved proteins with spherical polyelectrolyte brushes. In: Macromolecular Symposia. 2003, 191(1), pp. 81-88. ISSN 1022-1360. Available under: doi: 10.1002/masy.200390017deu
kops.citation.iso690WITTEMANN, Alexander, Björn HAUPT, R. MERKLE, Matthias BALLAUFF, 2003. Interaction of dissolved proteins with spherical polyelectrolyte brushes. In: Macromolecular Symposia. 2003, 191(1), pp. 81-88. ISSN 1022-1360. Available under: doi: 10.1002/masy.200390017eng
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    <dcterms:abstract xml:lang="eng">We consider the adsorption of bovine serum albumin (BSA) on spherical polyelectrolyte brushes (SPB). The SPB consist of a solid polystyrene core of 100nm diameter onto which linear polyelectrolyte chains (poly(acrylic acid), (PAA)) are grafted. The adsorption of BSA is studied at a pH of 6.1 at different concentrations of added salt and buffer (MES). We observe strong adsorption of BSA onto the SPB despite the effect that the particles as well as the dissolved BSA are charged negatively. The adsorption of BSA is strongest at low salt concentration and decreases drastically with increasing amounts of added salt. The adsorbed protein can be washed out again by raising the ionic strength. The various driving forces for the adsorption are discussed. It is demonstrated that the main driving force is located in the electrostatic interaction of the protein with the brush layer of the particles. All data show that the SPB present a new class of carrier particles whose interaction with proteins can be tuned in a well-defined manner.</dcterms:abstract>
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kops.sourcefieldMacromolecular Symposia. 2003, <b>191</b>(1), pp. 81-88. ISSN 1022-1360. Available under: doi: 10.1002/masy.200390017deu
kops.sourcefield.plainMacromolecular Symposia. 2003, 191(1), pp. 81-88. ISSN 1022-1360. Available under: doi: 10.1002/masy.200390017deu
kops.sourcefield.plainMacromolecular Symposia. 2003, 191(1), pp. 81-88. ISSN 1022-1360. Available under: doi: 10.1002/masy.200390017eng
kops.submitter.emailregina.fleischmann@uni-konstanz.dedeu
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source.periodicalTitleMacromolecular Symposia

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