dc.creatorPiccinini, Esteban
dc.creatorPallarola, Diego Andres
dc.creatorBattaglini, Fernando
dc.creatorAzzaroni, Omar
dc.date.accessioned2022-04-04T18:59:00Z
dc.date.accessioned2022-10-15T12:08:18Z
dc.date.available2022-04-04T18:59:00Z
dc.date.available2022-10-15T12:08:18Z
dc.date.created2022-04-04T18:59:00Z
dc.date.issued2015-08-07
dc.identifierPiccinini, Esteban; Pallarola, Diego Andres; Battaglini, Fernando; Azzaroni, Omar; Recognition-driven assembly of self-limiting supramolecular protein nanoparticles displaying enzymatic activity; Royal Society of Chemistry; Chemical Communications; 51; 07-8-2015; 14754-14757
dc.identifier1359-7345
dc.identifierhttp://hdl.handle.net/11336/154309
dc.identifier1364-548X
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4384278
dc.description.abstractWe report the recognition-driven assembly of self-limiting protein nanoparticles displaying enzymatic activity. Solution self-assembly of concanavalin A lectin and glycoenzyme glucose oxidase leads to the spontaneous formation of biocolloids with well-defined dimensions, narrow size distribution and remarkable stability. These biocolloids successfully recognize a glycosylated modified electrode retaining the enzyme activity.
dc.languageeng
dc.publisherRoyal Society of Chemistry
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1039/C5CC05837F
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://pubs.rsc.org/en/content/articlelanding/2015/CC/C5CC05837F
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectNANOPARTICLES
dc.subjectBIORECOGNITION
dc.subjectSELF-LIMITING ASSEMBLY
dc.subjectENZYMATIC ACTIVITY
dc.titleRecognition-driven assembly of self-limiting supramolecular protein nanoparticles displaying enzymatic activity
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersion


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