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dc.contributor.authorFrank, Julia
dc.contributor.authorRichter, Maximilian
dc.contributor.authorde Rossi, Chiara
dc.contributor.authorLehr, Claus-Michael
dc.contributor.authorFuhrmann, Kathrin
dc.contributor.authorFuhrmann, Gregor
dc.date.accessioned2018-09-17T07:54:12Z
dc.date.available2018-09-17T07:54:12Z
dc.date.issued2018-08-17
dc.identifier.issn2045-2322
dc.identifier.pmid30120298
dc.identifier.doi10.1038/s41598-018-30786-y
dc.identifier.urihttp://hdl.handle.net/10033/621482
dc.description.abstractExtracellular vesicles (EVs) are natural nanoparticles that play important roles in intercellular communication and are increasingly studied for biosignalling, pathogenesis and therapy. Nevertheless, little is known about optimal conditions for their transfer and storage, and the potential impact on preserving EV-loaded cargoes. We present the first comprehensive stability assessment of different widely available types of EVs during various storage conditions including -80 °C, 4 °C, room temperature, and freeze-drying (lyophilisation). Lyophilisation of EVs would allow easy handling at room temperature and thus significantly enhance their expanded investigation. A model enzyme, β-glucuronidase, was loaded into different types of EVs derived from mesenchymal stem cells, endothelial cells and cancer cells. Using asymmetric flow field-flow fractionation we proved that the model enzyme is indeed stably encapsulated into EVs. When assessing enzyme activity as indicator for EV stability, and in comparison to liposomes, we show that EVs are intrinsically stable during lyophilisation, an effect further enhanced by cryoprotectants. Our findings provide new insight for exploring lyophilisation as a novel storage modality and we create an important basis for standardised and advanced EV applications in biomedical research.en_US
dc.rightsAttribution-NonCommercial-ShareAlike 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/us/*
dc.titleExtracellular vesicles protect glucuronidase model enzymes during freeze-drying.en_US
dc.typeArticleen_US
dc.contributor.departmentHIPS, Helmholtz-Institut für pharmazeutische Forschung Saarland, Universitätscampus 8.1, 66123 Saarbrücken, Germany.en_US
refterms.dateFOA2018-09-17T07:54:13Z
dc.source.journaltitleScientific reports


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