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Issue 3, 2014
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Versatile multi-functionalization of protein nanofibrils for biosensor applications

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Abstract

Protein nanofibrils offer advantages over other nanostructures due to the ease in their self-assembly and the versatility of surface chemistry available. Yet, an efficient and general methodology for their post-assembly functionalization remains a significant challenge. We introduce a generic approach, based on biotinylation and thiolation, for the multi-functionalization of protein nanofibrils self-assembled from whey proteins. Biochemical characterization shows the effects of the functionalization onto the nanofibrils' surface, giving insights into the changes in surface chemistry of the nanostructures. We show how these methods can be used to decorate whey protein nanofibrils with several components such as fluorescent quantum dots, enzymes, and metal nanoparticles. A multi-functionalization approach is used, as a proof of principle, for the development of a glucose biosensor platform, where the protein nanofibrils act as nanoscaffolds for glucose oxidase. Biotinylation is used for enzyme attachment and thiolation for nanoscaffold anchoring onto a gold electrode surface. Characterization via cyclic voltammetry shows an increase in glucose-oxidase mediated current response due to thiol–metal interactions with the gold electrode. The presented approach for protein nanofibril multi-functionalization is novel and has the potential of being applied to other protein nanostructures with similar surface chemistry.

Graphical abstract: Versatile multi-functionalization of protein nanofibrils for biosensor applications

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Publication details

The article was received on 28 Oct 2013, accepted on 15 Nov 2013 and first published on 22 Nov 2013


Article type: Paper
DOI: 10.1039/C3NR05752F
Nanoscale, 2014,6, 1629-1634

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    Versatile multi-functionalization of protein nanofibrils for biosensor applications

    L. Sasso, S. Suei, L. Domigan, J. Healy, V. Nock, M. A. K. Williams and J. A. Gerrard, Nanoscale, 2014, 6, 1629
    DOI: 10.1039/C3NR05752F

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