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Interaction of proteins with spherical polyelectrolyte brushes in solution as studied by small-angle x-ray scattering

Interaction of proteins with spherical polyelectrolyte brushes in solution as studied by small-angle x-ray scattering

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ROSENFELDT, Sabine, Alexander WITTEMANN, Matthias BALLAUFF, Eugenia BREININGER, Jörg BOLZE, Nico DINGENOUTS, 2004. Interaction of proteins with spherical polyelectrolyte brushes in solution as studied by small-angle x-ray scattering. In: Physical Review E. 70(6). ISSN 1539-3755

@article{Rosenfeldt2004Inter-20211, title={Interaction of proteins with spherical polyelectrolyte brushes in solution as studied by small-angle x-ray scattering}, year={2004}, doi={10.1103/PhysRevE.70.061403}, number={6}, volume={70}, issn={1539-3755}, journal={Physical Review E}, author={Rosenfeldt, Sabine and Wittemann, Alexander and Ballauff, Matthias and Breininger, Eugenia and Bolze, Jörg and Dingenouts, Nico} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/20211"> <dc:contributor>Dingenouts, Nico</dc:contributor> <dc:rights>deposit-license</dc:rights> <dc:contributor>Bolze, Jörg</dc:contributor> <dc:contributor>Ballauff, Matthias</dc:contributor> <dcterms:title>Interaction of proteins with spherical polyelectrolyte brushes in solution as studied by small-angle x-ray scattering</dcterms:title> <dc:creator>Rosenfeldt, Sabine</dc:creator> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dcterms:abstract xml:lang="eng">We use small-angle x-ray scattering (SAXS) as a tool to study the binding of proteins to spherical polyelectrolyte brushes (SPB) in situ. The SPB consists of a solid core of ∼ 100 nm diam onto which long polyelectrolyte chains [poly(styrene sulfonic acid, PSS) and poly(acrylic acid, PAA)] have been densely grafted. The proteins used in this investigation, Bovine Serum Albumine (BSA) and Bovine Pancreatic Ribonuclease A (RNase A), adsorb strongly to these SPB if the ionic strength is low despite their negative charge. Virtually no adsorption takes place at high ionic strength. SAXS demonstrates that both proteins are distributed within the brush. The findings reported here give further evidence that the strong adsorption of proteins to SPB is due to the “counterions release forces”: The patches of positive charge on the surface of the proteins become multivalent counterions of the polyelectrolyte chains. Thus, a concomitant number of co- and counterions is thereby released and the entropy of the entire system is increased. The repulsive Coulombic interaction as well as the steric repulsion between the proteins and the brush layer are counterbalanced by this effect. The data discussed here demonstrate that the adsorption of proteins in SPB presents a new principle for the immobilization of proteins.</dcterms:abstract> <dc:creator>Dingenouts, Nico</dc:creator> <dc:creator>Bolze, Jörg</dc:creator> <dc:creator>Breininger, Eugenia</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-08-23T09:12:21Z</dc:date> <dc:creator>Ballauff, Matthias</dc:creator> <dc:contributor>Breininger, Eugenia</dc:contributor> <dc:contributor>Rosenfeldt, Sabine</dc:contributor> <dc:contributor>Wittemann, Alexander</dc:contributor> <dc:language>eng</dc:language> <dc:creator>Wittemann, Alexander</dc:creator> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/20211"/> <dcterms:bibliographicCitation>First publ. in: Physical Review E ; 70 (2004), 6. - 061403</dcterms:bibliographicCitation> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-08-23T09:12:21Z</dcterms:available> <dcterms:issued>2004</dcterms:issued> </rdf:Description> </rdf:RDF>

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Interaction of proteins with SPB as studied by SAXS_Phys Rev E 2004.pdf 109

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