In Situ Infrared Ellipsometry for Protein Adsorption Studies on Ultrathin Smart Polymer Brushes in Aqueous Environment

Kroning, Annika; Furchner, Andreas; Aulich, Dennis; Bittrich, Eva; Rauch, Sebastian; Uhlmann, Petra; Eichhorn, Klaus-Jochen; Seeber, Michael; Luzinov, Igor; Kilbey, S. Michael; Lokitz, Bradley S.; Minko, Sergiy; Hinrichs, Karsten

doi:10.1021/am5075997

In Situ Infrared Ellipsometry for Protein Adsorption Studies on Ultrathin Smart Polymer Brushes in Aqueous Environment

Journal Article · Tue Feb 10 00:00:00 EST 2015 · ACS Applied Materials and Interfaces

DOI:https://doi.org/10.1021/am5075997· OSTI ID:1286795

Kroning, Annika ^[1]; Furchner, Andreas ^[1]; Aulich, Dennis ^[1]; Bittrich, Eva ^[2]; Rauch, Sebastian ^[2]; Uhlmann, Petra ^[2]; Eichhorn, Klaus-Jochen ^[2]; Seeber, Michael ^[3]; Luzinov, Igor ^[3]; Kilbey, S. Michael ^[4]; Lokitz, Bradley S. ^[5]; Minko, Sergiy ^[6]; Hinrichs, Karsten ^[1]

Leibniz Inst. for Analytical sciences (ISAS), Berlin (Germany)
Leibniz Inst. of Polymer Research (IPF), Dresden (Germany)
Clemson Univ., SC (United States). School of Materials Science and Engineering
Univ. of Tennessee, Knoxville, TN (United States). Dept. of Chemistry and of Chemical Engineering
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Center for Nanophase Materials Science (CNMS)
Univ. of Georgia, Athens, GA (United States). Dept. of Chemistry

The protein-adsorbing and -repelling properties of various smart nanometer-thin polymer brushes with high potential for biosensing and biomedical applications are studied by in-situ infrared-spectroscopic ellipsometry (IRSE). IRSE as a highly sensitive non-destructive technique allows us to investigate protein adsorption on polymer brushes in aqueous environment in dependence of external stimuli like temperature and pH. These stimuli are, for instance, relevant in switchable mixed brushes containing poly(N-isopropyl acrylamide) and poly(acrylic acid), respectively. We use such brushes as model surfaces for controlling protein adsorption of human serum albumin and human fibrinogen. IRSE can distinguish between polymer-specific vibrational bands, which yield insights into the hydration state of the brushes, and changes in the protein-specific amide bands, which are related to changes of the protein secondary structure.

View Accepted Manuscript (DOE)

Research Organization:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). Center for Nanophase Materials Sciences (CNMS)

Sponsoring Organization:: German Research Foundation; National Science Foundation (NSF); USDOE Office of Science (SC)

Grant/Contract Number:: AC05-00OR22725

OSTI ID:: 1286795

Journal Information:: ACS Applied Materials and Interfaces, Journal Name: ACS Applied Materials and Interfaces Journal Issue: 23 Vol. 7; ISSN 1944-8244

Publisher:: American Chemical Society (ACS)Copyright Statement

Country of Publication:: United States

Language:: English

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36 MATERIALS SCIENCE
59 BASIC BIOLOGICAL SCIENCES
in situ infrared ellipsometry
infrared spectroscopy
polymer brushes
protein adsorption
solid−liquid interface
stimuli-responsive

In Situ Infrared Ellipsometry for Protein Adsorption Studies on Ultrathin Smart Polymer Brushes in Aqueous Environment

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