Recognition-driven assembly of self-limiting supramolecular protein nanoparticles displaying enzymatic activity
We 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...
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2015
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13597345_v51_n79_p14754_Piccinini http://hdl.handle.net/20.500.12110/paper_13597345_v51_n79_p14754_Piccinini |
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paper:paper_13597345_v51_n79_p14754_Piccinini2023-06-08T16:11:30Z Recognition-driven assembly of self-limiting supramolecular protein nanoparticles displaying enzymatic activity Pallarola, Diego Andrés Battaglini, Fernando concanavalin A glucose oxidase lectin mannose nanoparticle protein enzyme protein Article chemical modification controlled study electrode enzyme active site enzyme activity hydrodynamics protein aggregation protein assembly protein interaction static electricity stoichiometry Enzymes Nanoparticles Proteins We 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. © The Royal Society of Chemistry 2015. Fil:Pallarola, D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Battaglini, F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2015 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13597345_v51_n79_p14754_Piccinini http://hdl.handle.net/20.500.12110/paper_13597345_v51_n79_p14754_Piccinini |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
concanavalin A glucose oxidase lectin mannose nanoparticle protein enzyme protein Article chemical modification controlled study electrode enzyme active site enzyme activity hydrodynamics protein aggregation protein assembly protein interaction static electricity stoichiometry Enzymes Nanoparticles Proteins |
| spellingShingle |
concanavalin A glucose oxidase lectin mannose nanoparticle protein enzyme protein Article chemical modification controlled study electrode enzyme active site enzyme activity hydrodynamics protein aggregation protein assembly protein interaction static electricity stoichiometry Enzymes Nanoparticles Proteins Pallarola, Diego Andrés Battaglini, Fernando Recognition-driven assembly of self-limiting supramolecular protein nanoparticles displaying enzymatic activity |
| topic_facet |
concanavalin A glucose oxidase lectin mannose nanoparticle protein enzyme protein Article chemical modification controlled study electrode enzyme active site enzyme activity hydrodynamics protein aggregation protein assembly protein interaction static electricity stoichiometry Enzymes Nanoparticles Proteins |
| description |
We 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. © The Royal Society of Chemistry 2015. |
| author |
Pallarola, Diego Andrés Battaglini, Fernando |
| author_facet |
Pallarola, Diego Andrés Battaglini, Fernando |
| author_sort |
Pallarola, Diego Andrés |
| title |
Recognition-driven assembly of self-limiting supramolecular protein nanoparticles displaying enzymatic activity |
| title_short |
Recognition-driven assembly of self-limiting supramolecular protein nanoparticles displaying enzymatic activity |
| title_full |
Recognition-driven assembly of self-limiting supramolecular protein nanoparticles displaying enzymatic activity |
| title_fullStr |
Recognition-driven assembly of self-limiting supramolecular protein nanoparticles displaying enzymatic activity |
| title_full_unstemmed |
Recognition-driven assembly of self-limiting supramolecular protein nanoparticles displaying enzymatic activity |
| title_sort |
recognition-driven assembly of self-limiting supramolecular protein nanoparticles displaying enzymatic activity |
| publishDate |
2015 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13597345_v51_n79_p14754_Piccinini http://hdl.handle.net/20.500.12110/paper_13597345_v51_n79_p14754_Piccinini |
| work_keys_str_mv |
AT pallaroladiegoandres recognitiondrivenassemblyofselflimitingsupramolecularproteinnanoparticlesdisplayingenzymaticactivity AT battaglinifernando recognitiondrivenassemblyofselflimitingsupramolecularproteinnanoparticlesdisplayingenzymaticactivity |
| _version_ |
1768545613715079168 |