Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview

Autores
Corchero, José Luis; Favaro, Marianna T. P.; Márquez Martínez, Merce; Lascorz, Jara; Martínez Torró, Carlos; Sanchez, Julieta Maria; López Laguna, Hèctor; de Souza Ferreira, Luís Carlos; Vázquez, Esther; Ferrer Miralles, Neus; Villaverde Corrales, Antonio; Parladé, Eloi
Año de publicación
2023
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
By following simple protein engineering steps, recombinant proteins with promising applications in the field of drug delivery can be assembled in the form of functional materials of increasing complexity, either as nanoparticles or nanoparticle-leaking secretory microparticles. Among the suitable strategies for protein assembly, the use of histidine-rich tags in combination with coordinating divalent cations allows the construction of both categories of material out of pure polypeptide samples. Such molecular crosslinking results in chemically homogeneous protein particles with a defined composition, a fact that offers soft regulatory routes towards clinical applications for nanostructured protein-only drugs or for protein-based drug vehicles. Successes in the fabrication and final performance of these materials are expected, irrespective of the protein source. However, this fact has not yet been fully explored and confirmed. By taking the antigenic RBD domain of the SARS-CoV-2 spike glycoprotein as a model building block, we investigated the production of nanoparticles and secretory microparticles out of the versions of recombinant RBD produced by bacteria (Escherichia coli), insect cells (Sf9), and two different mammalian cell lines (namely HEK 293F and Expi293F). Although both functional nanoparticles and secretory microparticles were effectively generated in all cases, the technological and biological idiosyncrasy of each type of cell factory impacted the biophysical properties of the products. Therefore, the selection of a protein biofabrication platform is not irrelevant but instead is a significant factor in the upstream pipeline of protein assembly into supramolecular, complex, and functional materials.
Fil: Corchero, José Luis. Universitat Autònoma de Barcelona; España
Fil: Favaro, Marianna T. P.. Universitat Autònoma de Barcelona; España. Universidade de Sao Paulo; Brasil
Fil: Márquez Martínez, Merce. Universitat Autònoma de Barcelona; España
Fil: Lascorz, Jara. Universitat Autònoma de Barcelona; España
Fil: Martínez Torró, Carlos. Universitat Autònoma de Barcelona; España
Fil: Sanchez, Julieta Maria. Universitat Autònoma de Barcelona; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
Fil: López Laguna, Hèctor. Universitat Autònoma de Barcelona; España
Fil: de Souza Ferreira, Luís Carlos. Universidade de Sao Paulo; Brasil
Fil: Vázquez, Esther. Universitat Autònoma de Barcelona; España
Fil: Ferrer Miralles, Neus. Universitat Autònoma de Barcelona; España
Fil: Villaverde Corrales, Antonio. Universitat Autònoma de Barcelona; España
Fil: Parladé, Eloi. Universitat Autònoma de Barcelona; España
Materia
BIOMIMETICS
BUILDING BLOCKS
CELL FACTORY
MICROPARTICLES
NANOPARTICLES
PROTEIN MATERIALS
PROTEIN SECRETION
RECOMBINANT PROTEINS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/230949
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/230949
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative OverviewCorchero, José LuisFavaro, Marianna T. P.Márquez Martínez, MerceLascorz, JaraMartínez Torró, CarlosSanchez, Julieta MariaLópez Laguna, Hèctorde Souza Ferreira, Luís CarlosVázquez, EstherFerrer Miralles, NeusVillaverde Corrales, AntonioParladé, EloiBIOMIMETICSBUILDING BLOCKSCELL FACTORYMICROPARTICLESNANOPARTICLESPROTEIN MATERIALSPROTEIN SECRETIONRECOMBINANT PROTEINShttps://purl.org/becyt/ford/2.10https://purl.org/becyt/ford/2By following simple protein engineering steps, recombinant proteins with promising applications in the field of drug delivery can be assembled in the form of functional materials of increasing complexity, either as nanoparticles or nanoparticle-leaking secretory microparticles. Among the suitable strategies for protein assembly, the use of histidine-rich tags in combination with coordinating divalent cations allows the construction of both categories of material out of pure polypeptide samples. Such molecular crosslinking results in chemically homogeneous protein particles with a defined composition, a fact that offers soft regulatory routes towards clinical applications for nanostructured protein-only drugs or for protein-based drug vehicles. Successes in the fabrication and final performance of these materials are expected, irrespective of the protein source. However, this fact has not yet been fully explored and confirmed. By taking the antigenic RBD domain of the SARS-CoV-2 spike glycoprotein as a model building block, we investigated the production of nanoparticles and secretory microparticles out of the versions of recombinant RBD produced by bacteria (Escherichia coli), insect cells (Sf9), and two different mammalian cell lines (namely HEK 293F and Expi293F). Although both functional nanoparticles and secretory microparticles were effectively generated in all cases, the technological and biological idiosyncrasy of each type of cell factory impacted the biophysical properties of the products. Therefore, the selection of a protein biofabrication platform is not irrelevant but instead is a significant factor in the upstream pipeline of protein assembly into supramolecular, complex, and functional materials.Fil: Corchero, José Luis. Universitat Autònoma de Barcelona; EspañaFil: Favaro, Marianna T. P.. Universitat Autònoma de Barcelona; España. Universidade de Sao Paulo; BrasilFil: Márquez Martínez, Merce. Universitat Autònoma de Barcelona; EspañaFil: Lascorz, Jara. Universitat Autònoma de Barcelona; EspañaFil: Martínez Torró, Carlos. Universitat Autònoma de Barcelona; EspañaFil: Sanchez, Julieta Maria. Universitat Autònoma de Barcelona; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; ArgentinaFil: López Laguna, Hèctor. Universitat Autònoma de Barcelona; EspañaFil: de Souza Ferreira, Luís Carlos. Universidade de Sao Paulo; BrasilFil: Vázquez, Esther. Universitat Autònoma de Barcelona; EspañaFil: Ferrer Miralles, Neus. Universitat Autònoma de Barcelona; EspañaFil: Villaverde Corrales, Antonio. Universitat Autònoma de Barcelona; EspañaFil: Parladé, Eloi. Universitat Autònoma de Barcelona; EspañaMultidisciplinary Digital Publishing Institute (MDPI)2023-04-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/230949Corchero, José Luis; Favaro, Marianna T. P.; Márquez Martínez, Merce; Lascorz, Jara; Martínez Torró, Carlos; et al.; Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview; Multidisciplinary Digital Publishing Institute (MDPI); Pharmaceutics; 15; 4; 9-4-2023; 15041197: 1-161999-4923CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/pharmaceutics15041197info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1999-4923/15/4/1197info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:56:54Zoai:ri.conicet.gov.ar:11336/230949instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:56:54.963CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview
title Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview
spellingShingle Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview
Corchero, José Luis
BIOMIMETICS
BUILDING BLOCKS
CELL FACTORY
MICROPARTICLES
NANOPARTICLES
PROTEIN MATERIALS
PROTEIN SECRETION
RECOMBINANT PROTEINS
title_short Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview
title_full Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview
title_fullStr Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview
title_full_unstemmed Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview
title_sort Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview
dc.creator.none.fl_str_mv Corchero, José Luis
Favaro, Marianna T. P.
Márquez Martínez, Merce
Lascorz, Jara
Martínez Torró, Carlos
Sanchez, Julieta Maria
López Laguna, Hèctor
de Souza Ferreira, Luís Carlos
Vázquez, Esther
Ferrer Miralles, Neus
Villaverde Corrales, Antonio
Parladé, Eloi
author Corchero, José Luis
author_facet Corchero, José Luis
Favaro, Marianna T. P.
Márquez Martínez, Merce
Lascorz, Jara
Martínez Torró, Carlos
Sanchez, Julieta Maria
López Laguna, Hèctor
de Souza Ferreira, Luís Carlos
Vázquez, Esther
Ferrer Miralles, Neus
Villaverde Corrales, Antonio
Parladé, Eloi
author_role author
author2 Favaro, Marianna T. P.
Márquez Martínez, Merce
Lascorz, Jara
Martínez Torró, Carlos
Sanchez, Julieta Maria
López Laguna, Hèctor
de Souza Ferreira, Luís Carlos
Vázquez, Esther
Ferrer Miralles, Neus
Villaverde Corrales, Antonio
Parladé, Eloi
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv BIOMIMETICS
BUILDING BLOCKS
CELL FACTORY
MICROPARTICLES
NANOPARTICLES
PROTEIN MATERIALS
PROTEIN SECRETION
RECOMBINANT PROTEINS
topic BIOMIMETICS
BUILDING BLOCKS
CELL FACTORY
MICROPARTICLES
NANOPARTICLES
PROTEIN MATERIALS
PROTEIN SECRETION
RECOMBINANT PROTEINS
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.10
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv By following simple protein engineering steps, recombinant proteins with promising applications in the field of drug delivery can be assembled in the form of functional materials of increasing complexity, either as nanoparticles or nanoparticle-leaking secretory microparticles. Among the suitable strategies for protein assembly, the use of histidine-rich tags in combination with coordinating divalent cations allows the construction of both categories of material out of pure polypeptide samples. Such molecular crosslinking results in chemically homogeneous protein particles with a defined composition, a fact that offers soft regulatory routes towards clinical applications for nanostructured protein-only drugs or for protein-based drug vehicles. Successes in the fabrication and final performance of these materials are expected, irrespective of the protein source. However, this fact has not yet been fully explored and confirmed. By taking the antigenic RBD domain of the SARS-CoV-2 spike glycoprotein as a model building block, we investigated the production of nanoparticles and secretory microparticles out of the versions of recombinant RBD produced by bacteria (Escherichia coli), insect cells (Sf9), and two different mammalian cell lines (namely HEK 293F and Expi293F). Although both functional nanoparticles and secretory microparticles were effectively generated in all cases, the technological and biological idiosyncrasy of each type of cell factory impacted the biophysical properties of the products. Therefore, the selection of a protein biofabrication platform is not irrelevant but instead is a significant factor in the upstream pipeline of protein assembly into supramolecular, complex, and functional materials.
Fil: Corchero, José Luis. Universitat Autònoma de Barcelona; España
Fil: Favaro, Marianna T. P.. Universitat Autònoma de Barcelona; España. Universidade de Sao Paulo; Brasil
Fil: Márquez Martínez, Merce. Universitat Autònoma de Barcelona; España
Fil: Lascorz, Jara. Universitat Autònoma de Barcelona; España
Fil: Martínez Torró, Carlos. Universitat Autònoma de Barcelona; España
Fil: Sanchez, Julieta Maria. Universitat Autònoma de Barcelona; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina
Fil: López Laguna, Hèctor. Universitat Autònoma de Barcelona; España
Fil: de Souza Ferreira, Luís Carlos. Universidade de Sao Paulo; Brasil
Fil: Vázquez, Esther. Universitat Autònoma de Barcelona; España
Fil: Ferrer Miralles, Neus. Universitat Autònoma de Barcelona; España
Fil: Villaverde Corrales, Antonio. Universitat Autònoma de Barcelona; España
Fil: Parladé, Eloi. Universitat Autònoma de Barcelona; España
description By following simple protein engineering steps, recombinant proteins with promising applications in the field of drug delivery can be assembled in the form of functional materials of increasing complexity, either as nanoparticles or nanoparticle-leaking secretory microparticles. Among the suitable strategies for protein assembly, the use of histidine-rich tags in combination with coordinating divalent cations allows the construction of both categories of material out of pure polypeptide samples. Such molecular crosslinking results in chemically homogeneous protein particles with a defined composition, a fact that offers soft regulatory routes towards clinical applications for nanostructured protein-only drugs or for protein-based drug vehicles. Successes in the fabrication and final performance of these materials are expected, irrespective of the protein source. However, this fact has not yet been fully explored and confirmed. By taking the antigenic RBD domain of the SARS-CoV-2 spike glycoprotein as a model building block, we investigated the production of nanoparticles and secretory microparticles out of the versions of recombinant RBD produced by bacteria (Escherichia coli), insect cells (Sf9), and two different mammalian cell lines (namely HEK 293F and Expi293F). Although both functional nanoparticles and secretory microparticles were effectively generated in all cases, the technological and biological idiosyncrasy of each type of cell factory impacted the biophysical properties of the products. Therefore, the selection of a protein biofabrication platform is not irrelevant but instead is a significant factor in the upstream pipeline of protein assembly into supramolecular, complex, and functional materials.
publishDate 2023
dc.date.none.fl_str_mv 2023-04-09
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/230949
Corchero, José Luis; Favaro, Marianna T. P.; Márquez Martínez, Merce; Lascorz, Jara; Martínez Torró, Carlos; et al.; Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview; Multidisciplinary Digital Publishing Institute (MDPI); Pharmaceutics; 15; 4; 9-4-2023; 15041197: 1-16
1999-4923
CONICET Digital
CONICET
url http://hdl.handle.net/11336/230949
identifier_str_mv Corchero, José Luis; Favaro, Marianna T. P.; Márquez Martínez, Merce; Lascorz, Jara; Martínez Torró, Carlos; et al.; Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview; Multidisciplinary Digital Publishing Institute (MDPI); Pharmaceutics; 15; 4; 9-4-2023; 15041197: 1-16
1999-4923
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3390/pharmaceutics15041197
info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1999-4923/15/4/1197
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute (MDPI)
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute (MDPI)
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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