Structural and functional characteristics of chimeric avidins physically adsorbed onto functionalized polythiophene thin films

Willem M. Albers (Corresponding Author), Jani M. Pelto, Clément Suspène, Juha A. Määttä, Abderrahim Yassar, Vesa P. Hytönen, Inger M. Vikholm-Lundin, Kirsi Tappura

Research output: Contribution to journalArticleScientificpeer-review

10 Citations (Scopus)

Abstract

Stabilized bioreceptor layers are of great importance in the design of novel biosensors. In earlier work, chimeric avidins enabled immobilization of biotinylated antibodies onto gold surfaces with greater stability compared to more conventional avidins (wild-type avidin and streptavidin). In the present study, the applicability of chimeric avidins as a general binding scaffold for biotinylated antibodies on spin-coated functionalized polythiophene thin films has been studied by surface plasmon resonance and atomic force microscopy. Novel chimeric avidins showed remarkably increased binding characteristics compared with other avidins, such as wild-type avidin, streptavidin, and bacterial avidin when merely physically adsorbed onto the polythiophene surface. They gave the highest binding capacities, the highest affinity constant, and the highest stability for biotinylated probe immobilization. Introduction of carboxylic acid groups to polythiophene layer further enhanced the binding level of the avidins. Polythiophene layers functionalized with chimeric avidins thus offered a promising generic platform for biosensor applications.
Original languageEnglish
Pages (from-to)4067-4077
Number of pages10
JournalACS Applied Materials & Interfaces
Volume4
Issue number8
DOIs
Publication statusPublished - 2012
MoE publication typeA1 Journal article-refereed

Fingerprint

Avidin
Thin films
Polymers
Biosensors
Antibodies
Surface plasmon resonance
Scaffolds (biology)
Carboxylic acids
Streptavidin
Atomic force microscopy
Gold
polythiophene
Carboxylic Acids
Scaffolds

Keywords

  • Chimeric avidin
  • polythiophene
  • C-reactive protein
  • antibody immobilization
  • surface plasmon resonance
  • atomic force microscopy

Cite this

Albers, Willem M. ; Pelto, Jani M. ; Suspène, Clément ; Määttä, Juha A. ; Yassar, Abderrahim ; Hytönen, Vesa P. ; Vikholm-Lundin, Inger M. ; Tappura, Kirsi. / Structural and functional characteristics of chimeric avidins physically adsorbed onto functionalized polythiophene thin films. In: ACS Applied Materials & Interfaces. 2012 ; Vol. 4, No. 8. pp. 4067-4077.
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title = "Structural and functional characteristics of chimeric avidins physically adsorbed onto functionalized polythiophene thin films",
abstract = "Stabilized bioreceptor layers are of great importance in the design of novel biosensors. In earlier work, chimeric avidins enabled immobilization of biotinylated antibodies onto gold surfaces with greater stability compared to more conventional avidins (wild-type avidin and streptavidin). In the present study, the applicability of chimeric avidins as a general binding scaffold for biotinylated antibodies on spin-coated functionalized polythiophene thin films has been studied by surface plasmon resonance and atomic force microscopy. Novel chimeric avidins showed remarkably increased binding characteristics compared with other avidins, such as wild-type avidin, streptavidin, and bacterial avidin when merely physically adsorbed onto the polythiophene surface. They gave the highest binding capacities, the highest affinity constant, and the highest stability for biotinylated probe immobilization. Introduction of carboxylic acid groups to polythiophene layer further enhanced the binding level of the avidins. Polythiophene layers functionalized with chimeric avidins thus offered a promising generic platform for biosensor applications.",
keywords = "Chimeric avidin, polythiophene, C-reactive protein, antibody immobilization, surface plasmon resonance, atomic force microscopy",
author = "Albers, {Willem M.} and Pelto, {Jani M.} and Cl{\'e}ment Susp{\`e}ne and M{\"a}{\"a}tt{\"a}, {Juha A.} and Abderrahim Yassar and Hyt{\"o}nen, {Vesa P.} and Vikholm-Lundin, {Inger M.} and Kirsi Tappura",
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Structural and functional characteristics of chimeric avidins physically adsorbed onto functionalized polythiophene thin films. / Albers, Willem M. (Corresponding Author); Pelto, Jani M.; Suspène, Clément; Määttä, Juha A.; Yassar, Abderrahim; Hytönen, Vesa P.; Vikholm-Lundin, Inger M.; Tappura, Kirsi.

In: ACS Applied Materials & Interfaces, Vol. 4, No. 8, 2012, p. 4067-4077.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Structural and functional characteristics of chimeric avidins physically adsorbed onto functionalized polythiophene thin films

AU - Albers, Willem M.

AU - Pelto, Jani M.

AU - Suspène, Clément

AU - Määttä, Juha A.

AU - Yassar, Abderrahim

AU - Hytönen, Vesa P.

AU - Vikholm-Lundin, Inger M.

AU - Tappura, Kirsi

N1 - Project code: 36322 (EU-BioEGOFET)

PY - 2012

Y1 - 2012

N2 - Stabilized bioreceptor layers are of great importance in the design of novel biosensors. In earlier work, chimeric avidins enabled immobilization of biotinylated antibodies onto gold surfaces with greater stability compared to more conventional avidins (wild-type avidin and streptavidin). In the present study, the applicability of chimeric avidins as a general binding scaffold for biotinylated antibodies on spin-coated functionalized polythiophene thin films has been studied by surface plasmon resonance and atomic force microscopy. Novel chimeric avidins showed remarkably increased binding characteristics compared with other avidins, such as wild-type avidin, streptavidin, and bacterial avidin when merely physically adsorbed onto the polythiophene surface. They gave the highest binding capacities, the highest affinity constant, and the highest stability for biotinylated probe immobilization. Introduction of carboxylic acid groups to polythiophene layer further enhanced the binding level of the avidins. Polythiophene layers functionalized with chimeric avidins thus offered a promising generic platform for biosensor applications.

AB - Stabilized bioreceptor layers are of great importance in the design of novel biosensors. In earlier work, chimeric avidins enabled immobilization of biotinylated antibodies onto gold surfaces with greater stability compared to more conventional avidins (wild-type avidin and streptavidin). In the present study, the applicability of chimeric avidins as a general binding scaffold for biotinylated antibodies on spin-coated functionalized polythiophene thin films has been studied by surface plasmon resonance and atomic force microscopy. Novel chimeric avidins showed remarkably increased binding characteristics compared with other avidins, such as wild-type avidin, streptavidin, and bacterial avidin when merely physically adsorbed onto the polythiophene surface. They gave the highest binding capacities, the highest affinity constant, and the highest stability for biotinylated probe immobilization. Introduction of carboxylic acid groups to polythiophene layer further enhanced the binding level of the avidins. Polythiophene layers functionalized with chimeric avidins thus offered a promising generic platform for biosensor applications.

KW - Chimeric avidin

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KW - antibody immobilization

KW - surface plasmon resonance

KW - atomic force microscopy

U2 - 10.1021/am3008517

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JO - ACS Applied Materials & Interfaces

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