Graphene Biosensor Programming with Genetically Engineered Fusion Protein Monolayers

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A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä
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Date

2016-03-30

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Department of Biotechnology and Chemical Technology
Department of Bioproducts and Biosystems

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Language

en

Pages

8

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ACS Applied Materials and Interfaces, Volume 8, issue 12, pp. 8257-8264

Abstract

We demonstrate a label-free biosensor concept based on specific receptor modules, which provide immobilization and selectivity to the desired analyte molecules, and on charge sensing with a graphene field effect transistor. The receptor modules are fusion proteins in which small hydrophobin proteins act as the anchor to immobilize the receptor moiety. The functionalization of the graphene sensor is a single-step process based on directed self-assembly of the receptor modules on a hydrophobic surface. The modules are produced separately in fungi or plants and purified before use. The modules form a dense and well-oriented monolayer on the graphene transistor channel and the receptor module monolayer can be removed, and a new module monolayer with a different selectivity can be assembled in situ. The receptor module monolayers survive drying, showing that the functionalized devices can be stored and have a reasonable shelf life. The sensor is tested with small charged peptides and large immunoglobulin molecules. The measured sensitivities are in the femtomolar range, and the response is relatively fast, of the order of one second. (Graph Presented).

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Keywords

graphene, biosensor, fusion protein, hydrophobin, self-assembly, Debye length, CRYSTAL-STRUCTURES, HYDROPHOBIN HFBI, SENSORS, FUNCTIONALIZATION, PURIFICATION, FILMS

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DOI

10.1021/acsami.6b00123

Citation

Soikkeli, M, Kurppa, K, Kainlauri, M, Arpiainen, S, Paananen, A, Gunnarsson, D, Joensuu, J J, Laaksonen, P, Prunnila, M, Linder, M B & Ahopelto, J 2016, 'Graphene Biosensor Programming with Genetically Engineered Fusion Protein Monolayers', ACS Applied Materials and Interfaces, vol. 8, no. 12, pp. 8257-8264. https://doi.org/10.1021/acsami.6b00123

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https://urn.fi/URN:NBN:fi:aalto-202104206207

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[article-cris] Kemian tekniikan korkeakoulu / CHEM