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

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

doi:10.1021/am5075997

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

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

Center for Nanophase Matls Sciences

Research output: Contribution to journal › Article › peer-review

44 Scopus citations

Abstract

The protein-adsorbing and -repelling properties of various smart nanometer-thin polymer brushes containing poly(N-isopropylacrylamide) and poly(acrylic acid) with high potential for biosensing and biomedical applications are studied by in situ infrared-spectroscopic ellipsometry (IRSE). IRSE is a highly sensitive nondestructive technique that allows protein adsorption on polymer brushes to be investigated in an aqueous environment as external stimuli, such as temperature and pH, are varied. These changes are relevant to conditions for regulation of protein adsorption and desorption for biotechnology, biocatalysis, and bioanalytical applications. Here brushes are used as model surfaces for controlling protein adsorption of human serum albumin and human fibrinogen. The important finding of this work is that IRSE in the in situ experiments in protein solutions can distinguish between contributions of polymer brushes and proteins. The vibrational bands of the polymers provide insights into the hydration state of the brushes, whereas the protein-specific amide bands are related to changes of the protein secondary structure.

Original language	English
Pages (from-to)	12430-12439
Number of pages	10
Journal	ACS Applied Materials and Interfaces
Volume	7
Issue number	23
DOIs	https://doi.org/10.1021/am5075997
State	Published - Jun 17 2015

Funding

Funders	Funder number
National Science Foundation	1133320

Keywords

in situ infrared ellipsometry
infrared spectroscopy
polymer brushes
protein adsorption
solid-liquid interface
stimuli-responsive

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10.1021/am5075997

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Kroning, A., Furchner, A., Aulich, D., Bittrich, E., Rauch, S., Uhlmann, P., Eichhorn, K. J., Seeber, M., Luzinov, I., Kilbey, S. M., Lokitz, B. S., Minko, S., & Hinrichs, K. (2015). In Situ Infrared Ellipsometry for Protein Adsorption Studies on Ultrathin Smart Polymer Brushes in Aqueous Environment. ACS Applied Materials and Interfaces, 7(23), 12430-12439. https://doi.org/10.1021/am5075997

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

abstract = "The protein-adsorbing and -repelling properties of various smart nanometer-thin polymer brushes containing poly(N-isopropylacrylamide) and poly(acrylic acid) with high potential for biosensing and biomedical applications are studied by in situ infrared-spectroscopic ellipsometry (IRSE). IRSE is a highly sensitive nondestructive technique that allows protein adsorption on polymer brushes to be investigated in an aqueous environment as external stimuli, such as temperature and pH, are varied. These changes are relevant to conditions for regulation of protein adsorption and desorption for biotechnology, biocatalysis, and bioanalytical applications. Here brushes are used as model surfaces for controlling protein adsorption of human serum albumin and human fibrinogen. The important finding of this work is that IRSE in the in situ experiments in protein solutions can distinguish between contributions of polymer brushes and proteins. The vibrational bands of the polymers provide insights into the hydration state of the brushes, whereas the protein-specific amide bands are related to changes of the protein secondary structure.",

keywords = "in situ infrared ellipsometry, infrared spectroscopy, polymer brushes, protein adsorption, solid-liquid interface, stimuli-responsive",

author = "Annika Kroning and Andreas Furchner and Dennis Aulich and Eva Bittrich and Sebastian Rauch and Petra Uhlmann and Eichhorn, {Klaus Jochen} and Michael Seeber and Igor Luzinov and Kilbey, {S. Michael} and Lokitz, {Bradley S.} and Sergiy Minko and Karsten Hinrichs",

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year = "2015",

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doi = "10.1021/am5075997",

language = "English",

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Kroning, A, Furchner, A, Aulich, D, Bittrich, E, Rauch, S, Uhlmann, P, Eichhorn, KJ, Seeber, M, Luzinov, I, Kilbey, SM, Lokitz, BS, Minko, S & Hinrichs, K 2015, 'In Situ Infrared Ellipsometry for Protein Adsorption Studies on Ultrathin Smart Polymer Brushes in Aqueous Environment', ACS Applied Materials and Interfaces, vol. 7, no. 23, pp. 12430-12439. https://doi.org/10.1021/am5075997

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AU - Kroning, Annika

AU - Furchner, Andreas

AU - Aulich, Dennis

AU - Bittrich, Eva

AU - Rauch, Sebastian

AU - Uhlmann, Petra

AU - Eichhorn, Klaus Jochen

AU - Seeber, Michael

AU - Luzinov, Igor

AU - Kilbey, S. Michael

AU - Lokitz, Bradley S.

AU - Minko, Sergiy

AU - Hinrichs, Karsten

PY - 2015/6/17

Y1 - 2015/6/17

N2 - The protein-adsorbing and -repelling properties of various smart nanometer-thin polymer brushes containing poly(N-isopropylacrylamide) and poly(acrylic acid) with high potential for biosensing and biomedical applications are studied by in situ infrared-spectroscopic ellipsometry (IRSE). IRSE is a highly sensitive nondestructive technique that allows protein adsorption on polymer brushes to be investigated in an aqueous environment as external stimuli, such as temperature and pH, are varied. These changes are relevant to conditions for regulation of protein adsorption and desorption for biotechnology, biocatalysis, and bioanalytical applications. Here brushes are used as model surfaces for controlling protein adsorption of human serum albumin and human fibrinogen. The important finding of this work is that IRSE in the in situ experiments in protein solutions can distinguish between contributions of polymer brushes and proteins. The vibrational bands of the polymers provide insights into the hydration state of the brushes, whereas the protein-specific amide bands are related to changes of the protein secondary structure.

AB - The protein-adsorbing and -repelling properties of various smart nanometer-thin polymer brushes containing poly(N-isopropylacrylamide) and poly(acrylic acid) with high potential for biosensing and biomedical applications are studied by in situ infrared-spectroscopic ellipsometry (IRSE). IRSE is a highly sensitive nondestructive technique that allows protein adsorption on polymer brushes to be investigated in an aqueous environment as external stimuli, such as temperature and pH, are varied. These changes are relevant to conditions for regulation of protein adsorption and desorption for biotechnology, biocatalysis, and bioanalytical applications. Here brushes are used as model surfaces for controlling protein adsorption of human serum albumin and human fibrinogen. The important finding of this work is that IRSE in the in situ experiments in protein solutions can distinguish between contributions of polymer brushes and proteins. The vibrational bands of the polymers provide insights into the hydration state of the brushes, whereas the protein-specific amide bands are related to changes of the protein secondary structure.

KW - in situ infrared ellipsometry

KW - infrared spectroscopy

KW - polymer brushes

KW - protein adsorption

KW - solid-liquid interface

KW - stimuli-responsive

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

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