Protein adsorption on and swelling of polyelectrolyte brushes: A simultaneous ellipsometry-quartz crystal microbalance study.

Eva Bittrich, Keith Brian Rodenhausen, Klaus Jochen Eichhorn, Tino Hofmann, Mathias Schubert, Manfred Stamm, Petra Uhlmann

Research output: Contribution to journalArticle

63 Scopus citations

Abstract

With a coupled spectroscopic ellipsometry-quartz crystal microbalance with dissipation (QCM-D) experimental setup, quantitative information can be obtained about the amount of buffer components (water molecules and ions) coupled to a poly(acrylic acid) (PAA) brush surface in swelling and protein adsorption processes. PAA Guiselin brushes with more than one anchoring point per single polymer chain were prepared. For the swollen brushes a high amount of buffer was found to be coupled to the brush-solution interface in addition to the content of buffer inside the brush layer. Upon adsorption of bovine serum albumin the further incorporation of buffer molecules into the protein-brush layer was monitored at overall electrostatic attractive conditions [below the protein isolectric poimt (IEP)] and electrostatic repulsive conditions (above the protein IEP), and the shear viscosity of the combined polymer-protein layer was evaluated from QCM-D data. For adsorption at the "wrong side" of the IEP an incorporation of excess buffer molecules was observed, indicating an adjustment of charges in the combined polymer-protein layer. Desorption of protein at pH 7.6 led to a very high stretching of the polymer-protein layer with additional incorporation of high amounts of buffer, reflecting the increase of negative charges on the protein molecules at this elevated pH.

Original languageEnglish (US)
Pages (from-to)159-167
Number of pages9
JournalBiointerphases
Volume5
Issue number4
DOIs
Publication statusPublished - Dec 2010

    Fingerprint

ASJC Scopus subject areas

  • Chemistry(all)
  • Biomaterials
  • Materials Science(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

Cite this