Interactions of Catalytic Enzymes with n-Type Polymers for High-Performance Metabolite Sensors

David Ohayon; Dominik Renn; Shofarul Wustoni; Keying Guo; Victor Druet; Adel Hama; Xingxing Chen; Iuliana Petruta Maria; Saumya Singh; Sophie Griggs; Bob C. Schroeder; Magnus Rueping; Iain McCulloch; Sahika Inal

doi:10.1021/acsami.2c20502

Interactions of Catalytic Enzymes with n-Type Polymers for High-Performance Metabolite Sensors

David Ohayon, Dominik Renn, Shofarul Wustoni, Keying Guo, Victor Druet, Adel Hama, Xingxing Chen, Iuliana Petruta Maria, Saumya Singh, Sophie Griggs, Bob C. Schroeder, Magnus Rueping, Iain McCulloch, Sahika Inal^*

^*Corresponding author for this work

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

5 Scopus citations

Abstract

The tight regulation of the glucose concentration in the body is crucial for balanced physiological function. We developed an electrochemical transistor comprising an n-type conjugated polymer film in contact with a catalytic enzyme for sensitive and selective glucose detection in bodily fluids. Despite the promise of these sensors, the property of the polymer that led to such high performance has remained unknown, with charge transport being the only characteristic under focus. Here, we studied the impact of the polymer chemical structure on film surface properties and enzyme adsorption behavior using a combination of physiochemical characterization methods and correlated our findings with the resulting sensor performance. We developed five n-type polymers bearing the same backbone with side chains differing in polarity and charge. We found that the nature of the side chains modulated the film surface properties, dictating the extent of interactions between the enzyme and the polymer film. Quartz crystal microbalance with dissipation monitoring studies showed that hydrophobic surfaces retained more enzymes in a densely packed arrangement, while hydrophilic surfaces captured fewer enzymes in a flattened conformation. X-ray photoelectron spectroscopy analysis of the surfaces revealed strong interactions of the enzyme with the glycolated side chains of the polymers, which improved for linear side chains compared to those for branched ones. We probed the alterations in the enzyme structure upon adsorption using circular dichroism, which suggested protein denaturation on hydrophobic surfaces. Our study concludes that a negatively charged, smooth, and hydrophilic film surface provides the best environment for enzyme adsorption with desired mass and conformation, maximizing the sensor performance. This knowledge will guide synthetic work aiming to establish close interactions between proteins and electronic materials, which is crucial for developing high-performance enzymatic metabolite biosensors and biocatalytic charge-conversion devices.

Original language	English
Journal	ACS applied materials & interfaces
DOIs	https://doi.org/10.1021/acsami.2c20502
State	Accepted/In press - 2022
Externally published	Yes

Keywords

catalytic enzymes
conjugated polymers
electron transporting (n-type) polymers
enzymatic sensors
glucose
organic bioelectronics
organic electrochemical transistor

Access to Document

10.1021/acsami.2c20502

Cite this

@article{5bb1a2b4b2be473a9f8e077183ca849c,

title = "Interactions of Catalytic Enzymes with n-Type Polymers for High-Performance Metabolite Sensors",

abstract = "The tight regulation of the glucose concentration in the body is crucial for balanced physiological function. We developed an electrochemical transistor comprising an n-type conjugated polymer film in contact with a catalytic enzyme for sensitive and selective glucose detection in bodily fluids. Despite the promise of these sensors, the property of the polymer that led to such high performance has remained unknown, with charge transport being the only characteristic under focus. Here, we studied the impact of the polymer chemical structure on film surface properties and enzyme adsorption behavior using a combination of physiochemical characterization methods and correlated our findings with the resulting sensor performance. We developed five n-type polymers bearing the same backbone with side chains differing in polarity and charge. We found that the nature of the side chains modulated the film surface properties, dictating the extent of interactions between the enzyme and the polymer film. Quartz crystal microbalance with dissipation monitoring studies showed that hydrophobic surfaces retained more enzymes in a densely packed arrangement, while hydrophilic surfaces captured fewer enzymes in a flattened conformation. X-ray photoelectron spectroscopy analysis of the surfaces revealed strong interactions of the enzyme with the glycolated side chains of the polymers, which improved for linear side chains compared to those for branched ones. We probed the alterations in the enzyme structure upon adsorption using circular dichroism, which suggested protein denaturation on hydrophobic surfaces. Our study concludes that a negatively charged, smooth, and hydrophilic film surface provides the best environment for enzyme adsorption with desired mass and conformation, maximizing the sensor performance. This knowledge will guide synthetic work aiming to establish close interactions between proteins and electronic materials, which is crucial for developing high-performance enzymatic metabolite biosensors and biocatalytic charge-conversion devices.",

keywords = "catalytic enzymes, conjugated polymers, electron transporting (n-type) polymers, enzymatic sensors, glucose, organic bioelectronics, organic electrochemical transistor",

author = "David Ohayon and Dominik Renn and Shofarul Wustoni and Keying Guo and Victor Druet and Adel Hama and Xingxing Chen and Maria, {Iuliana Petruta} and Saumya Singh and Sophie Griggs and Schroeder, {Bob C.} and Magnus Rueping and Iain McCulloch and Sahika Inal",

note = "Publisher Copyright: {\textcopyright} 2023 American Chemical Society.",

year = "2022",

doi = "10.1021/acsami.2c20502",

language = "英语",

journal = "ACS applied materials & interfaces",

issn = "1944-8244",

publisher = "American Chemical Society",

}

TY - JOUR

T1 - Interactions of Catalytic Enzymes with n-Type Polymers for High-Performance Metabolite Sensors

AU - Ohayon, David

AU - Renn, Dominik

AU - Wustoni, Shofarul

AU - Guo, Keying

AU - Druet, Victor

AU - Hama, Adel

AU - Chen, Xingxing

AU - Maria, Iuliana Petruta

AU - Singh, Saumya

AU - Griggs, Sophie

AU - Schroeder, Bob C.

AU - Rueping, Magnus

AU - McCulloch, Iain

AU - Inal, Sahika

PY - 2022

Y1 - 2022

N2 - The tight regulation of the glucose concentration in the body is crucial for balanced physiological function. We developed an electrochemical transistor comprising an n-type conjugated polymer film in contact with a catalytic enzyme for sensitive and selective glucose detection in bodily fluids. Despite the promise of these sensors, the property of the polymer that led to such high performance has remained unknown, with charge transport being the only characteristic under focus. Here, we studied the impact of the polymer chemical structure on film surface properties and enzyme adsorption behavior using a combination of physiochemical characterization methods and correlated our findings with the resulting sensor performance. We developed five n-type polymers bearing the same backbone with side chains differing in polarity and charge. We found that the nature of the side chains modulated the film surface properties, dictating the extent of interactions between the enzyme and the polymer film. Quartz crystal microbalance with dissipation monitoring studies showed that hydrophobic surfaces retained more enzymes in a densely packed arrangement, while hydrophilic surfaces captured fewer enzymes in a flattened conformation. X-ray photoelectron spectroscopy analysis of the surfaces revealed strong interactions of the enzyme with the glycolated side chains of the polymers, which improved for linear side chains compared to those for branched ones. We probed the alterations in the enzyme structure upon adsorption using circular dichroism, which suggested protein denaturation on hydrophobic surfaces. Our study concludes that a negatively charged, smooth, and hydrophilic film surface provides the best environment for enzyme adsorption with desired mass and conformation, maximizing the sensor performance. This knowledge will guide synthetic work aiming to establish close interactions between proteins and electronic materials, which is crucial for developing high-performance enzymatic metabolite biosensors and biocatalytic charge-conversion devices.

AB - The tight regulation of the glucose concentration in the body is crucial for balanced physiological function. We developed an electrochemical transistor comprising an n-type conjugated polymer film in contact with a catalytic enzyme for sensitive and selective glucose detection in bodily fluids. Despite the promise of these sensors, the property of the polymer that led to such high performance has remained unknown, with charge transport being the only characteristic under focus. Here, we studied the impact of the polymer chemical structure on film surface properties and enzyme adsorption behavior using a combination of physiochemical characterization methods and correlated our findings with the resulting sensor performance. We developed five n-type polymers bearing the same backbone with side chains differing in polarity and charge. We found that the nature of the side chains modulated the film surface properties, dictating the extent of interactions between the enzyme and the polymer film. Quartz crystal microbalance with dissipation monitoring studies showed that hydrophobic surfaces retained more enzymes in a densely packed arrangement, while hydrophilic surfaces captured fewer enzymes in a flattened conformation. X-ray photoelectron spectroscopy analysis of the surfaces revealed strong interactions of the enzyme with the glycolated side chains of the polymers, which improved for linear side chains compared to those for branched ones. We probed the alterations in the enzyme structure upon adsorption using circular dichroism, which suggested protein denaturation on hydrophobic surfaces. Our study concludes that a negatively charged, smooth, and hydrophilic film surface provides the best environment for enzyme adsorption with desired mass and conformation, maximizing the sensor performance. This knowledge will guide synthetic work aiming to establish close interactions between proteins and electronic materials, which is crucial for developing high-performance enzymatic metabolite biosensors and biocatalytic charge-conversion devices.

KW - catalytic enzymes

KW - conjugated polymers

KW - electron transporting (n-type) polymers

KW - enzymatic sensors

KW - glucose

KW - organic bioelectronics

KW - organic electrochemical transistor

UR - http://www.scopus.com/inward/record.url?scp=85147808742&partnerID=8YFLogxK

U2 - 10.1021/acsami.2c20502

DO - 10.1021/acsami.2c20502

M3 - 文章

AN - SCOPUS:85147808742

SN - 1944-8244

JO - ACS applied materials & interfaces

JF - ACS applied materials & interfaces

ER -

Interactions of Catalytic Enzymes with n-Type Polymers for High-Performance Metabolite Sensors

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this