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

Research output: Contribution to journalArticleScientificpeer-review


Original languageEnglish
Pages (from-to)4067-4077
Number of pages11
JournalACS Applied Materials and Interfaces
Issue number8
Publication statusPublished - 22 Aug 2012
Publication typeA1 Journal article-refereed


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.

ASJC Scopus subject areas


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