Wiring of Redox Enzymes on Three Dimensional Self-Assembled Molecular Scaffold

The integration of biological molecules and nanoscale components provides a fertile basis for the construction of hybrid materials of synergic properties and functions. Stable protein 1 (SP1), a highly stable ring shaped protein, was recently used to display different functional domains, to bind nan...

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Bibliographic Details
Published inLangmuir Vol. 27; no. 20; pp. 12606 - 12613
Main Authors Frasconi, Marco, Heyman, Arnon, Medalsy, Izhar, Porath, Danny, Mazzei, Franco, Shoseyov, Oded
Format Journal Article
LanguageEnglish
Published Washington, DC American Chemical Society 18.10.2011
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Summary:The integration of biological molecules and nanoscale components provides a fertile basis for the construction of hybrid materials of synergic properties and functions. Stable protein 1 (SP1), a highly stable ring shaped protein, was recently used to display different functional domains, to bind nanoparticles (NPs), and to spontaneously form two and three-dimensional structures. Here we show an approach to wire redox enzymes on this self-assembled protein–nanoparticle hybrid. Those hybrids are genetically engineered SP1s, displaying glucose oxidase (GOx) enzymes tethered to the protein inner pore. Moreover, the Au-NP–protein hybrids self-assembled to multiple enzymatic layers on the surface. By wiring the redox enzymes to the electrode, we present an active structure for the bioelectrocatalytic oxidation of glucose. This system demonstrates for the first time a three-dimensional assembly of multiple catalytic modules on a protein scaffold with an efficient electrical wiring of the enzyme units on an electrode surface, thus implementing a hybrid electrically active unit for nanobioelectronic applications.
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ISSN:0743-7463
1520-5827
DOI:10.1021/la2020435