α-Galactosidase-A loaded-nanoliposomes with enhanced enzymatic activity and intracellular penetration
Mostra el registre complet Registre parcial de l'ítem
- dc.contributor.author Cabrera, Ingrid
- dc.contributor.author Abasolo, Ibane
- dc.contributor.author Corchero, José L.
- dc.contributor.author Elizondo, Elisa
- dc.contributor.author Rivera Gil, Pilar, 1976-
- dc.contributor.author Moreno, Evelyn
- dc.contributor.author Faraudo, Jordi
- dc.contributor.author Sala, Santi
- dc.contributor.author Bueno, Dolores
- dc.contributor.author González Mira, Elisabet
- dc.contributor.author Rivas, Merche
- dc.contributor.author Melgarejo, Marta
- dc.contributor.author Pulido, Daniel
- dc.contributor.author Albericio, Fernando
- dc.contributor.author Royo, Miriam
- dc.contributor.author Villaverde, Antonio
- dc.contributor.author García Parajó, María F.
- dc.contributor.author Schwartz Jr, Simó
- dc.contributor.author Ventosa, Nora
- dc.contributor.author Veciana, Jaume
- dc.date.accessioned 2024-07-11T11:24:00Z
- dc.date.available 2024-07-11T11:24:00Z
- dc.date.issued 2016
- dc.description.abstract Lysosomal storage disorders (LSD) are caused by lysosomal dysfunction usually as a consequence of deficiency of a single enzyme required for the metabolism of macromolecules, such as lipids, glycoproteins, and mucopolysaccharides. For instance, the lack of α-galactosidase A (GLA) activity in Fabry disease patients causes the accumulation of glycosphingolipids in the vasculature leading to multiple organ pathology. Enzyme replacement therapy, which is the most common treatment of LSD, exhibits several drawbacks mainly related to the instability and low efficacy of the exogenously administered therapeutic enzyme. In this work, the unprecedented increased enzymatic activity and intracellular penetration achieved by the association of a human recombinant GLA to nanoliposomes functionalized with Arginine-Glycine-Aspartic acid (RGD) peptides is reported. Moreover, these new GLA loaded nanoliposomes lead to a higher efficacy in the reduction of the GLA substrate named globotriasylceramide in a cellular model of Fabry disease, than that achieved by the same concentration of the free enzyme. The preparation of these new liposomal formulations by DELOS-SUSP, based on the depressurization of a CO2 -expanded liquid organic solution, shows the great potential of this CO2 -based methodology for the one-step production of protein-nanoliposome conjugates as bioactive nanomaterials with therapeutic interest.
- dc.format.mimetype application/pdf
- dc.identifier.citation Cabrera I, Abasolo I, Corchero JL, Elizondo E, Rivera Gil P, Moreno E, et al. α-Galactosidase-A loaded-nanoliposomes with enhanced enzymatic activity and intracellular penetration. Adv Healthc Mater. 2016 Apr 6;5(7):829-40. DOI: 10.1002/adhm.201500746
- dc.identifier.doi http://dx.doi.org/10.1002/adhm.201500746
- dc.identifier.issn 2192-2640
- dc.identifier.uri http://hdl.handle.net/10230/60730
- dc.language.iso eng
- dc.publisher Wiley
- dc.relation.ispartof Adv Healthc Mater. 2016 Apr 6;5(7):829-40
- dc.rights This is the peer reviewed version of the following article: Cabrera I, Abasolo I, Corchero JL, Elizondo E, Gil PR, Moreno E, et al. α-Galactosidase-A loaded-nanoliposomes with enhanced enzymatic activity and intracellular penetration. Adv Healthc Mater. 2016 Apr 6;5(7):829-40. DOI: 10.1002/adhm.201500746, which has been published in final form at http://dx.doi.org/10.1002/adhm.201500746. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.
- dc.rights.accessRights info:eu-repo/semantics/openAccess
- dc.subject.keyword Fabry disease
- dc.subject.keyword RGD targeting
- dc.subject.keyword Compressed CO2
- dc.subject.keyword Nanoliposomes
- dc.subject.keyword α-galactosidase A
- dc.title α-Galactosidase-A loaded-nanoliposomes with enhanced enzymatic activity and intracellular penetration
- dc.type info:eu-repo/semantics/article
- dc.type.version info:eu-repo/semantics/acceptedVersion