Interaction of Proteins with a Planar Poly(acrylic acid) Brush: Analysis by Quartz Crystal Microbalance with Dissipation Monitoring (QCM-D)

Jacek Walkowiak; Michael Gradzielski; Stefan Zauscher; Matthias Ballauff

doi:10.3390/polym13010122

Interaction of Proteins with a Planar Poly(acrylic acid) Brush: Analysis by Quartz Crystal Microbalance with Dissipation Monitoring (QCM-D)

Jacek Walkowiak, Michael Gradzielski, Stefan Zauscher^*, Matthias Ballauff^*

^*Corresponding author for this work

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

Abstract

We describe the preparation of a poly(acrylic acid) (PAA) brush, polymerized by atom transfer radical polymerization (ATRP) of tert-butyl acrylate (tBA) and subsequent acid hydrolysis, on the flat gold surfaces of quartz-crystal microbalance (QCM) crystals. The PAA brushes were characterized by Fourier transform infrared (FT-IR) spectroscopy, ellipsometry and water contact angle analysis. The interaction of the PAA brushes with human serum albumin (HSA) was studied for a range of ionic strengths and pH conditions by quartz-crystal microbalance with dissipation monitoring (QCM-D). The quantitative analysis showed a strong adsorption of protein molecules onto the PAA brush. By increasing the ionic strength, we were able to release a fraction of the initially bound HSA molecules. This finding highlights the importance of counterions in the polyelectrolyte-mediated protein adsorption/desorption. A comparison with recent calorimetric studies related to the binding of HSA to polyelectrolytes allowed us to fully analyze the QCM data based on the results of the thermodynamic analysis of the binding process.

Original language	English
Article number	122
Number of pages	15
Journal	Polymers
Volume	13
Issue number	1
DOIs	https://doi.org/10.3390/polym13010122
Publication status	Published - Jan 2021

Keywords

polyelectrolyte brush
protein
ATRP
QCM-D
SPHERICAL POLYELECTROLYTE BRUSHES
TRANSFER RADICAL POLYMERIZATION
BLOCK-COPOLYMERS
VISCOELASTIC PROPERTIES
SERUM-ALBUMIN
ADSORPTION
POLYMERS
SURFACES
BEHAVIOR
ROUTE
Polyelectrolyte brush
Protein

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title = "Interaction of Proteins with a Planar Poly(acrylic acid) Brush: Analysis by Quartz Crystal Microbalance with Dissipation Monitoring (QCM-D)",

abstract = "We describe the preparation of a poly(acrylic acid) (PAA) brush, polymerized by atom transfer radical polymerization (ATRP) of tert-butyl acrylate (tBA) and subsequent acid hydrolysis, on the flat gold surfaces of quartz-crystal microbalance (QCM) crystals. The PAA brushes were characterized by Fourier transform infrared (FT-IR) spectroscopy, ellipsometry and water contact angle analysis. The interaction of the PAA brushes with human serum albumin (HSA) was studied for a range of ionic strengths and pH conditions by quartz-crystal microbalance with dissipation monitoring (QCM-D). The quantitative analysis showed a strong adsorption of protein molecules onto the PAA brush. By increasing the ionic strength, we were able to release a fraction of the initially bound HSA molecules. This finding highlights the importance of counterions in the polyelectrolyte-mediated protein adsorption/desorption. A comparison with recent calorimetric studies related to the binding of HSA to polyelectrolytes allowed us to fully analyze the QCM data based on the results of the thermodynamic analysis of the binding process.",

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author = "Jacek Walkowiak and Michael Gradzielski and Stefan Zauscher and Matthias Ballauff",

note = "Funding Information: Funding: We are grateful for financial support from the Deutsche Forschungsgemeinschaft via the International Research Training Group 1524 and for financial support from National Science Foundation Research Triangle Materials Research Science and Engineering Center (NSF MRSEC, DMR-11211107). Publisher Copyright: {\textcopyright} 2020 by the authors. Licensee MDPI, Basel, Switzerland.",

year = "2021",

month = jan,

doi = "10.3390/polym13010122",

language = "English",

volume = "13",

journal = "Polymers",

issn = "2073-4360",

publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",

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T1 - Interaction of Proteins with a Planar Poly(acrylic acid) Brush

T2 - Analysis by Quartz Crystal Microbalance with Dissipation Monitoring (QCM-D)

AU - Walkowiak, Jacek

AU - Gradzielski, Michael

AU - Zauscher, Stefan

AU - Ballauff, Matthias

N1 - Funding Information: Funding: We are grateful for financial support from the Deutsche Forschungsgemeinschaft via the International Research Training Group 1524 and for financial support from National Science Foundation Research Triangle Materials Research Science and Engineering Center (NSF MRSEC, DMR-11211107). Publisher Copyright: © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

PY - 2021/1

Y1 - 2021/1

N2 - We describe the preparation of a poly(acrylic acid) (PAA) brush, polymerized by atom transfer radical polymerization (ATRP) of tert-butyl acrylate (tBA) and subsequent acid hydrolysis, on the flat gold surfaces of quartz-crystal microbalance (QCM) crystals. The PAA brushes were characterized by Fourier transform infrared (FT-IR) spectroscopy, ellipsometry and water contact angle analysis. The interaction of the PAA brushes with human serum albumin (HSA) was studied for a range of ionic strengths and pH conditions by quartz-crystal microbalance with dissipation monitoring (QCM-D). The quantitative analysis showed a strong adsorption of protein molecules onto the PAA brush. By increasing the ionic strength, we were able to release a fraction of the initially bound HSA molecules. This finding highlights the importance of counterions in the polyelectrolyte-mediated protein adsorption/desorption. A comparison with recent calorimetric studies related to the binding of HSA to polyelectrolytes allowed us to fully analyze the QCM data based on the results of the thermodynamic analysis of the binding process.

AB - We describe the preparation of a poly(acrylic acid) (PAA) brush, polymerized by atom transfer radical polymerization (ATRP) of tert-butyl acrylate (tBA) and subsequent acid hydrolysis, on the flat gold surfaces of quartz-crystal microbalance (QCM) crystals. The PAA brushes were characterized by Fourier transform infrared (FT-IR) spectroscopy, ellipsometry and water contact angle analysis. The interaction of the PAA brushes with human serum albumin (HSA) was studied for a range of ionic strengths and pH conditions by quartz-crystal microbalance with dissipation monitoring (QCM-D). The quantitative analysis showed a strong adsorption of protein molecules onto the PAA brush. By increasing the ionic strength, we were able to release a fraction of the initially bound HSA molecules. This finding highlights the importance of counterions in the polyelectrolyte-mediated protein adsorption/desorption. A comparison with recent calorimetric studies related to the binding of HSA to polyelectrolytes allowed us to fully analyze the QCM data based on the results of the thermodynamic analysis of the binding process.

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KW - TRANSFER RADICAL POLYMERIZATION

KW - BLOCK-COPOLYMERS

KW - VISCOELASTIC PROPERTIES

KW - SERUM-ALBUMIN

KW - ADSORPTION

KW - POLYMERS

KW - SURFACES

KW - BEHAVIOR

KW - ROUTE

KW - Polyelectrolyte brush

KW - Protein

U2 - 10.3390/polym13010122

DO - 10.3390/polym13010122

M3 - Article

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SN - 2073-4360

VL - 13

JO - Polymers

JF - Polymers

IS - 1

M1 - 122

ER -

Interaction of Proteins with a Planar Poly(acrylic acid) Brush: Analysis by Quartz Crystal Microbalance with Dissipation Monitoring (QCM-D)

Abstract

Keywords

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