Journal
BIOINTERPHASES
Volume 5, Issue 4, Pages 1-9Publisher
AVS
DOI: 10.1116/1.3530841
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Funding
- German Science Foundation (DFG) [Sta 324/28-1, Ei 317/5-1]
- Procter Gamble Company
- J. A. Woollam Company, Inc.
- Nebraska NSF-EPSCoR
- University of Nebraska-Lincoln College of Engineering
- EPSCoR
- Office Of The Director [1004094] Funding Source: National Science Foundation
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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. (C) 2010 American Vacuum Society. [DOI: 10.1116/1.3530841]
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