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 Citations (Scopus)

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
StatePublished - Dec 2010

Fingerprint

Quartz Crystal Microbalance Techniques
Quartz crystal microbalances
Ellipsometry
brushes
Brushes
quartz crystals
Polyelectrolytes
swelling
microbalances
Adsorption
ellipsometry
Swelling
proteins
Proteins
adsorption
Buffers
buffers
Polymers
Molecules
carbopol 940

ASJC Scopus subject areas

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

Cite this

Protein adsorption on and swelling of polyelectrolyte brushes : A simultaneous ellipsometry-quartz crystal microbalance study. / Bittrich, Eva; Rodenhausen, Keith Brian; Eichhorn, Klaus Jochen; Hofmann, Tino; Schubert, Mathias; Stamm, Manfred; Uhlmann, Petra.

In: Biointerphases, Vol. 5, No. 4, 12.2010, p. 159-167.

Research output: Contribution to journalArticle

Bittrich, Eva ; Rodenhausen, Keith Brian ; Eichhorn, Klaus Jochen ; Hofmann, Tino ; Schubert, Mathias ; Stamm, Manfred ; Uhlmann, Petra. / Protein adsorption on and swelling of polyelectrolyte brushes : A simultaneous ellipsometry-quartz crystal microbalance study. In: Biointerphases. 2010 ; Vol. 5, No. 4. pp. 159-167.
@article{a64821cb23c749238f5a86283877690a,
title = "Protein adsorption on and swelling of polyelectrolyte brushes: A simultaneous ellipsometry-quartz crystal microbalance study.",
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.",
author = "Eva Bittrich and Rodenhausen, {Keith Brian} and Eichhorn, {Klaus Jochen} and Tino Hofmann and Mathias Schubert and Manfred Stamm and Petra Uhlmann",
year = "2010",
month = "12",
doi = "10.1116/1.3530841",
language = "English (US)",
volume = "5",
pages = "159--167",
journal = "Biointerphases",
issn = "1559-4106",
publisher = "American Vacuum Society",
number = "4",

}

TY - JOUR

T1 - Protein adsorption on and swelling of polyelectrolyte brushes

T2 - A simultaneous ellipsometry-quartz crystal microbalance study.

AU - Bittrich, Eva

AU - Rodenhausen, Keith Brian

AU - Eichhorn, Klaus Jochen

AU - Hofmann, Tino

AU - Schubert, Mathias

AU - Stamm, Manfred

AU - Uhlmann, Petra

PY - 2010/12

Y1 - 2010/12

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=79956327241&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79956327241&partnerID=8YFLogxK

U2 - 10.1116/1.3530841

DO - 10.1116/1.3530841

M3 - Article

C2 - 21219037

AN - SCOPUS:79956327241

VL - 5

SP - 159

EP - 167

JO - Biointerphases

JF - Biointerphases

SN - 1559-4106

IS - 4

ER -