1.
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14 p, 1.2 MB |
Extracellular vesicles from recombinant cell factories improve the activity and efficacy of enzymes defective in lysosomal storage disorders
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Seras-Franzoso, Joaquin (Biomaterials and Nanomedicine (CIBER-BBN)) ;
Díaz Riascos, Zamira Vanessa (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Corchero Nieto, José Luis (Universitat Autònoma de Barcelona) ;
González, Patricia (Biomaterials and Nanomedicine (CIBER-BBN)) ;
García Aranda, Natalia (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Mandaña, Mònica (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Riera, Roger (Institut de Bioenginyeria de Catalunya) ;
Boullosa, Ana (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Mancilla, Sandra (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Grayston, Alba (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Moltó-Abad, Marc (Hospital Universitari Vall d'Hebron) ;
Garcia-Fruitos, Elena (Universitat Autònoma de Barcelona) ;
Mendoza, Rosa (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Pintos-Morell, Guillem (Hospital Universitari Vall d'Hebron) ;
Albertazzi, Lorenzo (Institut de Bioenginyeria de Catalunya) ;
Rosell, Anna (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Casas, Josefina (Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas) ;
Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Schwartz, Simó (Biomaterials and Nanomedicine (CIBER-BBN)) ;
Abasolo, Ibane (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia)
In the present study the use of extracellular vesicles (EVs) as vehicles for therapeutic enzymes in lysosomal storage disorders was explored. EVs were isolated from mammalian cells overexpressing alpha-galactosidase A (GLA) or N-sulfoglucosamine sulfohydrolase (SGSH) enzymes, defective in Fabry and Sanfilippo A diseases, respectively. [...]
2021 - 10.1002/jev2.12058
Journal of extracellular vesicles, Vol. 10 (march 2021)
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2.
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9 p, 3.5 MB |
Tolerability to non-endosomal, micron-scale cell penetration probed with magnetic particles
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Ruiz-Cánovas, Eugènia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Mendoza, Rosa (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Corchero Nieto, José Luis (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
The capability of HeLa cells to internalize large spherical microparticles has been evaluated by using inorganic, magnetic microparticles of 1 and 2. 8 µm of diameter. In both absence but especially under the action of a magnet, both types of particles were uptaken, in absence of cytotoxicity, by a significant percentage of cells, in a non-endosomal process clearly favored by the magnetic field. [...]
2021 - 10.1016/j.colsurfb.2021.112123
Colloids and Surfaces B: Biointerfaces, Vol. 208 (December 2021) , art. 112123
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3.
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17 p, 1.2 MB |
Human α-galactosidase a mutants : Priceless tools to develop novel therapies for fabry disease
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Modrego, Andrea (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Amaranto, Marilla (Universidad Nacional de Córdoba (Argentina)) ;
Godino, Agustina (Universidad Nacional de Córdoba (Argentina)) ;
Mendoza, Rosa (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Barra, José Luis (Universidad Nacional de Córdoba (Argentina)) ;
Corchero Nieto, José Luis (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia)
Fabry disease (FD) is a lysosomal storage disease caused by mutations in the gene for the α-galactosidase A (GLA) enzyme. The absence of the enzyme or its activity results in the accumulation of glycosphingolipids, mainly globotriaosylceramide (Gb3), in different tissues, leading to a wide range of clinical manifestations. [...]
2021 - 10.3390/ijms22126518
International journal of molecular sciences, Vol. 22, Issue 12 (June 2021) , art. 6518
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4.
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15 p, 7.1 MB |
Application of Quality by Design to the robust preparation of a liposomal GLA formulation by DELOS-susp method
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Merlo-Mas, Josep (Nanomol Technologies S.L.) ;
Tomsen-Melero, Judit (Institut de Ciència de Materials de Barcelona) ;
Corchero Nieto, José Luis (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
González-Mira, Elisabet (Institut de Ciència de Materials de Barcelona) ;
Font, Albert (Leanbio S.L.) ;
Pedersen, Jannik N. (Aarhus University. Department of Chemistry and Interdisciplinary Nanoscience Center (iNANO) (Denmark)) ;
García Aranda, Natalia (Hospital Universitari Vall d'Hebron. Institut de Recerca) ;
Cristóbal-Lecina, Edgar (Institut de Química Avançada de Catalunya) ;
Alcaina-Hernando, Marta (Nanomol Technologies S.L.) ;
Mendoza, Rosa (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Garcia-Fruitos, Elena (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Lizarraga, Teresa (Leanbio S.L.) ;
Resch, Susanne (BioNanoNet Forschungsgesellschaft mbH (Austria)) ;
Schimpel, Christa (BioNanoNet Forschungsgesellschaft mbH (Austria)) ;
Falk, Andreas (BioNanoNet Forschungsgesellschaft mbH (Austria)) ;
Pulido, Daniel (Institut de Química Avançada de Catalunya) ;
Royo, Miriam (Institut de Química Avançada de Catalunya) ;
Schwartz, Simó (Hospital Universitari Vall d'Hebron. Institut de Recerca) ;
Abasolo, Ibane (Hospital Universitari Vall d'Hebron. Institut de Recerca) ;
Pedersen, Jan Skov (Aarhus University. Department of Chemistry and Interdisciplinary Nanoscience Center (iNANO) (Denmark)) ;
Danino, Dganit (Technion - Israel Institute of Technology. CryoEM Laboratory of Soft Matter) ;
Soldevila, Andreu (Leanbio S.L.) ;
Veciana, Jaume (Institut de Ciència de Materials de Barcelona) ;
Sala, Santi (Nanomol Technologies S.L.) ;
Ventosa, Nora (Institut de Ciència de Materials de Barcelona) ;
Córdoba, Alba (Nanomol Technologies S.L.)
Fabry disease is a lysosomal storage disease arising from a deficiency of the enzyme α-galactosidase A (GLA). The enzyme deficiency results in an accumulation of glycolipids, which over time, leads to cardiovascular, cerebrovascular, and renal disease, ultimately leading to death in the fourth or fifth decade of life. [...]
2021 - 10.1016/j.supflu.2021.105204
The Journal of Supercritical Fluids, Vol. 173 (July 2021) , art. 105204
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5.
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6.
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1 p, 682.3 KB |
Erratum to : Detoxifying Escherichia coli for endotoxin-free production of recombinant proteins
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Mamat, Uwe (Leibniz-Center for Medicine and Biosciences. Division of Structural Biochemistry) ;
Wilke, Kathleen (Leibniz-Center for Medicine and Biosciences. Division of Structural Biochemistry) ;
Bramhill, David (Bramhill Biological Consulting. East Moonstone Drive) ;
Schromm, Andra Beate (Leibniz-Center for Medicine and Biosciences. Division of Structural Biochemistry) ;
Lindner, Buko (Leibniz-Center for Medicine and Biosciences. Division of Structural Biochemistry) ;
Kohl, Thomas Andreas (Leibniz-Center for Medicine and Biosciences. Division of Structural Biochemistry) ;
Corchero Nieto, José Luis (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Villaverde Corrales, Antonio (Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina) ;
Schaffer, Lana (The Scripps Research Institute) ;
Head, Steven Robert (The Scripps Research Institute) ;
Souvignier, Chad (Research Corporation Technologies (Tucson)) ;
Meredith, Timothy Charles (Pennsylvania State University. Department of Biochemistry and Molecular Biology) ;
Woodard, Ronald Wesley (University of Michigan. Department of Medicinal Chemistry)
2015 - 10.1186/s12934-015-0265-x
Microbial cell factories, Vol. 14, Issue 57 (2015)
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7.
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12 p, 5.7 MB |
Intracellular CXCR4 + cell targeting with T22-empowered protein-only nanoparticles
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Unzueta Elorza, Ugutz (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Céspedes, María Virtudes (Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina) ;
Ferrer-Miralles, Neus (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Casanova Rigat, Isolda (Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina) ;
Cedano, Juan (Laboratory of Immunology, Regional Norte, Universidad de la Republica, Salto, Uruguay) ;
Corchero Nieto, José Luis (Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina) ;
Domingo-Espin, Joan (Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina) ;
Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Mangues, Ramon (Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina) ;
Vázquez Gómez, Esther (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Universitat Autònoma de Barcelona.
Departament de Genètica i de Microbiologia
Cell-targeting peptides or proteins are appealing tools in nanomedicine and innovative medicines because they increase the local drug concentration and reduce potential side effects. CXC chemokine receptor 4 (CXCR4) is a cell surface marker associated with several severe human pathologies, including colorectal cancer, for which intracellular targeting agents are currently missing. [...]
2012 - 10.2147/IJN.S34450
International Journal of Nanomedicine, Vol. 7 (august 2012) , p. 4533-4544
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8.
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5 p, 470.7 KB |
Packaging protein drugs as bacterial inclusion bodies for therapeutic applications
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Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Garcia-Fruitos, Elena (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Rinas, Ursula (Helmholtz-Zentrum für Infektionsforschung) ;
Seras-Franzoso, Joaquin (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Kosoy, Ana (Janus Development SL) ;
Corchero Nieto, José Luis (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Vázquez Gómez, Esther (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Universitat Autònoma de Barcelona.
Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí"
A growing number of insights on the biology of bacterial inclusion bodies (IBs) have revealed intriguing utilities of these protein particles. Since they combine mechanical stability and protein functionality, IBs have been already exploited in biocatalysis and explored for bottom-up topographical modification in tissue engineering. [...]
2012 - 10.1186/1475-2859-11-76
Microbial cell factories, Vol. 11 (June 2012) , art. 76
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9.
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5 p, 243.9 KB |
Biological activities of histidine-rich peptides; merging biotechnology and nanomedicine
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Ferrer-Miralles, Neus (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Corchero Nieto, José Luis (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia) ;
Kumar, Pradeep (CSIR-Institute of Genomics and Integrative Biology) ;
Cedano Rodríguez, Juan Antonio (Universidad de la República (Uruguay).) ;
Gupta, Kailash C (CSIR-Indian Institute of Toxicology Research) ;
Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ;
Vázquez Gómez, Esther (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia)
Histidine-rich peptides are commonly used in recombinant protein production as purification tags, allowing the one-step affinity separation of the His-tagged proteins from the extracellular media or cell extracts. [...]
2011 - 10.1186/1475-2859-10-101
Microbial cell factories, Vol. 10 (2011) , art. 101
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