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hal.structure.identifierRadboud University [Nijmegen]
dc.contributor.authorPILLE, Jan
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorCARDINALE, Daniela
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorCARETTE, Noelle
hal.structure.identifierARN : régulations naturelle et artificielle
dc.contributor.authorDI PRIMO, Carmelo
dc.contributor.authorBESONG-NDIKA, Jane
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorWALTER, Jocelyne
hal.structure.identifierUnité de Pathologie Végétale [PV]
dc.contributor.authorLECOQ, Hervé
hal.structure.identifierRadboud University [Nijmegen]
dc.contributor.authorVAN ELDIJK, Mark B
hal.structure.identifierRadboud University [Nijmegen]
dc.contributor.authorSMITS, Ferdinanda C M
hal.structure.identifierRadboud University [Nijmegen]
dc.contributor.authorSCHOFFELEN, Sanne
hal.structure.identifierRadboud University [Nijmegen]
dc.contributor.authorVAN HEST, Jan C M
hal.structure.identifierHelsingin yliopisto = Helsingfors universitet = University of Helsinki
dc.contributor.authorMAKINEN, Kristiina
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorMICHON, Thierry
dc.date.issued2013
dc.identifier.issn1525-7797
dc.description.abstractEnHere we develop a novel approach allowing the noncovalent assembly of proteins on well-defined nanoscaffolds such as virus particles. The antibody-binding peptide Z33 was genetically fused to the monomeric yellow fluorescent protein and 4-coumarate:CoA-ligase 2. This Z33 "tag" allowed their patterning on the surface of zucchini yellow mosaic virus by means of specific antibodies directed against the coat protein of the virus. The approach was validated by affinity assays and correlative microscopy. The coverage efficiency was ∼87%. Fluorescence and enzymatic activity were fully retained after assembly. The principle of using the combination of a scaffold-specific antibody and Z33-fusion proteins can be extended to a wide variety of proteins/enzymes and antigenic scaffolds to support coupling for creating functional "biochips" with optical or catalytic properties.
dc.language.isoen
dc.publisherAmerican Chemical Society
dc.title.enGeneral strategy for ordered noncovalent protein assembly on well-defined nanoscaffolds
dc.typeArticle de revue
dc.identifier.doi10.1021/bm401291u
dc.subject.halSciences du Vivant [q-bio]/Autre [q-bio.OT]
bordeaux.journalBiomacromolecules
bordeaux.page4351-4359
bordeaux.volume14
bordeaux.issue12
bordeaux.peerReviewedoui
hal.identifierhal-02645827
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02645827v1
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