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Engineered PQQ-Glucose Dehydrogenase as a Universal Biosensor Platform.

Guo, Zhong and Murphy, Lindy and Stein, Viktor and Johnston, Wayne A. and Alcala-Perez, Siro and Alexandrov, Kirill (2016):
Engineered PQQ-Glucose Dehydrogenase as a Universal Biosensor Platform.
In: Journal of the American Chemical Society, pp. 10108-11, 138, (32), ISSN 1520-5126, [Article]

Abstract

Biosensors with direct electron output hold promise for nearly seamless integration with portable electronic devices. However, so far, they have been based on naturally occurring enzymes that significantly limit the spectrum of detectable analytes. Here, we present a novel biosensor architecture based on analyte-driven intermolecular recombination and activity reconstitution of a re-engineered component of glucometers: PQQ-glucose dehydrogenase. We demonstrate that this sensor architecture can be rapidly adopted for the detection of immunosuppressant drugs, α-amylase protein, or protease activity of thrombin and Factor Xa. The biosensors could be stored in dried form without appreciable loss of activity. We further show that ligand-induced activity of the developed biosensors could be directly monitored by chronoamperometry, enabling construction of disposable sensory electrodes. We expect that this architecture could be expanded to the detection of other biochemical activities, post-translational modifications, nucleic acids, and inorganic molecules.

Item Type: Article
Erschienen: 2016
Creators: Guo, Zhong and Murphy, Lindy and Stein, Viktor and Johnston, Wayne A. and Alcala-Perez, Siro and Alexandrov, Kirill
Title: Engineered PQQ-Glucose Dehydrogenase as a Universal Biosensor Platform.
Language: English
Abstract:

Biosensors with direct electron output hold promise for nearly seamless integration with portable electronic devices. However, so far, they have been based on naturally occurring enzymes that significantly limit the spectrum of detectable analytes. Here, we present a novel biosensor architecture based on analyte-driven intermolecular recombination and activity reconstitution of a re-engineered component of glucometers: PQQ-glucose dehydrogenase. We demonstrate that this sensor architecture can be rapidly adopted for the detection of immunosuppressant drugs, α-amylase protein, or protease activity of thrombin and Factor Xa. The biosensors could be stored in dried form without appreciable loss of activity. We further show that ligand-induced activity of the developed biosensors could be directly monitored by chronoamperometry, enabling construction of disposable sensory electrodes. We expect that this architecture could be expanded to the detection of other biochemical activities, post-translational modifications, nucleic acids, and inorganic molecules.

Journal or Publication Title: Journal of the American Chemical Society
Volume: 138
Number: 32
Divisions: 10 Department of Biology > Protein Engineering of Ion Conducting Nanopores
10 Department of Biology
Date Deposited: 14 Nov 2016 10:52
Identification Number: doi:10.1021/jacs.6b06342
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