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TitleVersatile multi-functionalization of protein nanofibrils for biosensor applications
Publication TypeJournal Article
Year of Publication2014
AuthorsSasso, L., Suei S., Domigan L., Healy J., Nock V., Williams M.A.K., and Gerrard J.A.
Pagination1629 - 1634
Date Published2014
ISSN20403364 (ISSN)
Keywordsacylation, amine, Amines, article, Atomic force microscopy, Biochemical characterization, Biosensing Techniques, Biosensor applications, biotin, biotinylation, chemistry, cross linking reagent, Cross-Linking Reagents, Cyclic voltammetry, Electrochemistry, electrode, Electrodes, Fluorescent quantum dots, Functionalizations, General methodologies, genetic procedures, glucose, Glucose oxidase, Glucose sensors, Gold, metal nanoparticle, Metal Nanoparticles, methodology, Microscopy, Atomic Force, Microscopy, Electron, Transmission, milk protein, Milk proteins, Multi-functionalization, Nanofibers, Nanostructures, Nanotechnology, Proof of principles, Protein nanofibrils, Proteins, Quantum Dot, Quantum Dots, Streptavidin, Sulfhydryl Compounds, Surface chemistry, Surface properties, surface property, thiol derivative, Transmission electron microscopy, whey protein
AbstractProtein 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. © 2013 The Royal Society of Chemistry.

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