Engineered self-assembling monolayers for label free detection of influenza nucleoprotein

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dc.contributor.authorLe Brun, APen_AU
dc.contributor.authorSoliakov, Aen_AU
dc.contributor.authorShah, DSHen_AU
dc.contributor.authorHolt, SAen_AU
dc.contributor.authorMcGill, Aen_AU
dc.contributor.authorAlison, JHen_AU
dc.date.accessioned2025-01-09T04:30:58Zen_AU
dc.date.available2025-01-09T04:30:58Zen_AU
dc.date.issued2015-06en_AU
dc.date.statistics2024-09-03en_AU
dc.descriptionFunding from Technology Strategy Board grant (TSB/100565) to Orla Protein Technologies Ltd and Newcastle University for the ‘Virasens’ project and Wellcome Trust Grant Number 093581. The authors thank the Bragg Institute Programme Advisory Committee (proposal P1500), and the ISIS Facility Access Panel (RB121134), for the award of neutron beam time. APLB acknowledges a Discovery Early Career Researcher Award from the Australian Research Council (DE140101788). The authors thank Marie Gillon (ANSTO) and Helen Ridley (Newcastle University) for technical assistance.en_AU
dc.description.abstractIntegrating nanotechnology into useable devices requires a combination of bottom up and top down methodology. Often the techniques to measure and control these different components are entirely different, so methods that can analyse the nanoscale component in situ are of increasing importance. Here we describe a strategy that employs a self-assembling monolayer of engineered protein chimeras to display an array of oriented antibodies (IgG) on a microelectronic device for the label free detection of influenza nucleoprotein. The structural and functional properties of the bio-interface were characterised by a range of physical techniques including surface plasmon resonance, quartz-crystal microbalance and neutron reflectometry. This combination of methods reveals a 13.5 nm thick engineered-monolayer that (i) self-assembles on gold surfaces, (ii) captures IgG with high affinity in a defined orientation and (iii) specifically recognises the influenza A nucleoprotein. Furthermore we also show that this non-covalent self-assembled structure can render the dissociation of bound IgG irreversible by chemical crosslinking in situ without affecting the IgG function. The methods can thus describe in detail the transition from soluble engineered molecules with nanometre dimensions to an array that demonstrates the principles of a working influenza sensor. © The Author(s) 2015. Open Access. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.en_AU
dc.format.mediumPrinten_AU
dc.identifier.articlenumber49en_AU
dc.identifier.citationLe Brun, A. P., Soliakov, A., Shah, D. S. H., Holt, S. A., McGill, A., & Lakey, J. H. (2015). Engineered self-assembling monolayers for label free detection of influenza nucleoprotein. Biomedical Microdevices, 17(3), 49. doi.org/10.1007/s10544-015-9951-zen_AU
dc.identifier.issn1387-2176en_AU
dc.identifier.issn1572-8781en_AU
dc.identifier.issue3en_AU
dc.identifier.journaltitleBiomedical Microdevicesen_AU
dc.identifier.urihttps://doi.org/10.1007/s10544-015-9951-zen_AU
dc.identifier.urihttps://apo.ansto.gov.au/handle/10238/15867en_AU
dc.identifier.volume17en_AU
dc.languageEnglishen_AU
dc.language.isoenen_AU
dc.publisherSpringer Natureen_AU
dc.subjectInfluenzaen_AU
dc.subjectNanotechnologyen_AU
dc.subjectProtein engineeringen_AU
dc.subjectAntibodiesen_AU
dc.subjectNucleoproteinsen_AU
dc.subjectPlasmonsen_AU
dc.subjectQuartzen_AU
dc.subjectMicrobalancesen_AU
dc.subjectNeutron radiographyen_AU
dc.subjectQuartzen_AU
dc.titleEngineered self-assembling monolayers for label free detection of influenza nucleoproteinen_AU
dc.typeJournal Articleen_AU
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