Publikation:

Salt-induced protein resistance of polyelectrolyte brushes studied using fluorescence correlation spectroscopy and neutron reflectometry

Lade...
Vorschaubild

Dateien

Wittemann_Salt-induced_edit.pdf
Wittemann_Salt-induced_edit.pdfGröße: 2.87 MBDownloads: 324

Datum

2004

Autor:innen

Czeslik, Claus
Jackler, Guido
Hazlett, T.
Gratton, Enrico
Steitz, Roland
Ballauff, Matthias

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

DOI (zitierfähiger Link)
ArXiv-ID

Internationale Patentnummer

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung
Open Access Green
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

Physical Chemistry Chemical Physics. 2004, 6(24), pp. 5557-5563. ISSN 1463-9076. Available under: doi: 10.1039/B410805A

Zusammenfassung

We used two-photon excitation fluorescence correlation spectroscopy (FCS) and neutron reflectometry to study in situ the effect of salt concentration on the degree of protein binding to polyelectrolyte brushes. The binding of bovine serum albumin (BSA) to poly(acrylic acid) (PAA) brushes was characterized at neutral pH values where both the protein and the brushes carry a negative charge. Spherical PAA brush particles were used in the FCS experiments, whereas a planar PAA brush served as protein substrate in the neutron reflectometry experiments. It has been found that BSA binds strongly to both the spherical and the planar PAA brushes under electrostatic repulsion at low ionic strength. The BSA volume fraction profile, as determined from the neutron reflectivities, indicates a deep penetration of the BSA molecules into the PAA brush. However, the analysis of the FCS data reveals that the protein affinity of the spherical PAA brush particles decreases drastically when increasing the concentration of sodium chloride to a few 100 mM. This observation is in line with the measured neutron reflectivities of the planar PAA brush. The reflectivity curve obtained in the absence of protein is virtually overlapping with that measured when the PAA brush is in contact with a BSA solution but containing 500 mM sodium chloride which suggests protein resistance of the planar PAA brush at this elevated salt concentration. The results of this study provide evidence for a new kind of protein-resistant interfaces. Whereas protein binding to the PAA brush is likely to be dominated by the release of counterions, this driving force vanishes as the ionic strength of the solution is raised and protein molecules are repelled from the interface by steric interactions. In a general view, the “switching” of the protein affinity of a PAA brush by varying the ionic strength of the protein solution over a relatively small range may appear to be useful for biotechnological applications.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
540 Chemie

Schlagwörter

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690CZESLIK, Claus, Guido JACKLER, T. HAZLETT, Enrico GRATTON, Roland STEITZ, Alexander WITTEMANN, Matthias BALLAUFF, 2004. Salt-induced protein resistance of polyelectrolyte brushes studied using fluorescence correlation spectroscopy and neutron reflectometry. In: Physical Chemistry Chemical Physics. 2004, 6(24), pp. 5557-5563. ISSN 1463-9076. Available under: doi: 10.1039/B410805A
BibTex
@article{Czeslik2004Salti-20216,
  year={2004},
  doi={10.1039/B410805A},
  title={Salt-induced protein resistance of polyelectrolyte brushes studied using fluorescence correlation spectroscopy and neutron reflectometry},
  number={24},
  volume={6},
  issn={1463-9076},
  journal={Physical Chemistry Chemical Physics},
  pages={5557--5563},
  author={Czeslik, Claus and Jackler, Guido and Hazlett, T. and Gratton, Enrico and Steitz, Roland and Wittemann, Alexander and Ballauff, Matthias}
}
RDF
<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/20216">
    <dc:contributor>Czeslik, Claus</dc:contributor>
    <dcterms:bibliographicCitation>First publ. in: Physical Chemistry Chemical Physics ; 24 (2004), 6. - pp. 5557-5563</dcterms:bibliographicCitation>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:creator>Hazlett, T.</dc:creator>
    <dc:contributor>Steitz, Roland</dc:contributor>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:creator>Wittemann, Alexander</dc:creator>
    <dcterms:title>Salt-induced protein resistance of polyelectrolyte brushes studied using fluorescence correlation spectroscopy and neutron reflectometry</dcterms:title>
    <dc:contributor>Gratton, Enrico</dc:contributor>
    <dc:contributor>Jackler, Guido</dc:contributor>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/20216"/>
    <dc:rights>terms-of-use</dc:rights>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/20216/1/Wittemann_Salt-induced_edit.pdf"/>
    <dcterms:abstract xml:lang="eng">We used two-photon excitation fluorescence correlation spectroscopy (FCS) and neutron reflectometry to study in situ the effect of salt concentration on the degree of protein binding to polyelectrolyte brushes. The binding of bovine serum albumin (BSA) to poly(acrylic acid) (PAA) brushes was characterized at neutral pH values where both the protein and the brushes carry a negative charge. Spherical PAA brush particles were used in the FCS experiments, whereas a planar PAA brush served as protein substrate in the neutron reflectometry experiments. It has been found that BSA binds strongly to both the spherical and the planar PAA brushes under electrostatic repulsion at low ionic strength. The BSA volume fraction profile, as determined from the neutron reflectivities, indicates a deep penetration of the BSA molecules into the PAA brush. However, the analysis of the FCS data reveals that the protein affinity of the spherical PAA brush particles decreases drastically when increasing the concentration of sodium chloride to a few 100 mM. This observation is in line with the measured neutron reflectivities of the planar PAA brush. The reflectivity curve obtained in the absence of protein is virtually overlapping with that measured when the PAA brush is in contact with a BSA solution but containing 500 mM sodium chloride which suggests protein resistance of the planar PAA brush at this elevated salt concentration. The results of this study provide evidence for a new kind of protein-resistant interfaces. Whereas protein binding to the PAA brush is likely to be dominated by the release of counterions, this driving force vanishes as the ionic strength of the solution is raised and protein molecules are repelled from the interface by steric interactions. In a general view, the “switching” of the protein affinity of a PAA brush by varying the ionic strength of the protein solution over a relatively small range may appear to be useful for biotechnological applications.</dcterms:abstract>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/20216/1/Wittemann_Salt-induced_edit.pdf"/>
    <dc:contributor>Ballauff, Matthias</dc:contributor>
    <dc:language>eng</dc:language>
    <dc:creator>Jackler, Guido</dc:creator>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-08-23T12:14:01Z</dc:date>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:issued>2004</dcterms:issued>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:creator>Ballauff, Matthias</dc:creator>
    <dc:contributor>Wittemann, Alexander</dc:contributor>
    <dc:creator>Steitz, Roland</dc:creator>
    <dc:contributor>Hazlett, T.</dc:contributor>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dc:creator>Czeslik, Claus</dc:creator>
    <dc:creator>Gratton, Enrico</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-08-23T12:14:01Z</dcterms:available>
  </rdf:Description>
</rdf:RDF>

Interner Vermerk

xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter

Kontakt
URL der Originalveröffentl.

Prüfdatum der URL

Prüfungsdatum der Dissertation

Finanzierungsart

Kommentar zur Publikation

Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Nein
Begutachtet
Diese Publikation teilen