Lyophilization of biomimetic amyloids preserves their regulatable, endocrine-like functions for nanoparticle release

Autores
TP Favaro, Marianna; López Laguna, Hèctor; Voltà Durán, Eric; Alba Castellon, Lorena; Sanchez, Julieta Maria; Casanova, Isolda; Unzueta, Ugutz; Mangues, Ramón; Villaverde, Antonio; Vázquez, Esther
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The secretory granules from the mammalian endocrine system are functional amyloids that act as dynamic depots to store and release protein hormones into the bloodstream. The controlled in vitro coordination between divalent cations and solvent-exposed histidine residues triggers reversible, cross-molecular interactions that result in granular protein aggregates with protein-leaking properties. While these synthetic particles are mechanically stable, they progressively disintegrate and release their protein building blocks, mimicking the performance of secretory granules. Envisaged as delivery systems for endocrine-like, time-sustained protein release, their clinical applicability should be supported by robust storage procedures, so far unset. Being lyophilization a desirable storage method for protein drugs, how this procedure could preserve the performance of clinically oriented functional amyloids is a neglected issue. We have here explored, tailored and validated lyophilization as an industrially and clinically friendly, fully scalable approach to the storage of functional amyloids aimed at secretion of protein-only nanoparticles. By doing so, protein-protein interactions in such materials have been characterized, and citrate identified as an efficient modulator of the temporal secretion profile, through which the sustainability of the leaking process can be finely regulated.
Fil: TP Favaro, Marianna. Universitat Autònoma de Barcelona; España
Fil: López Laguna, Hèctor. Universitat Autònoma de Barcelona; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Voltà Durán, Eric. Universitat Autònoma de Barcelona; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Alba Castellon, Lorena. Institut de Recerca Sant Pau; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España. Josep Carreras Leukaemia Research Institute; España
Fil: Sanchez, Julieta Maria. 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. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; Argentina. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España. Universitat Autònoma de Barcelona; España
Fil: Casanova, Isolda. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España. Institut de Recerca Sant Pau; España. Josep Carreras Leukaemia Research Institute; España
Fil: Unzueta, Ugutz. Josep Carreras Leukaemia Research Institute; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España. Institut de Recerca Sant Pau; España
Fil: Mangues, Ramón. Josep Carreras Leukaemia Research Institute; España. Institut de Recerca Sant Pau; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Villaverde, Antonio. Universitat Autònoma de Barcelona; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Vázquez, Esther. Universitat Autònoma de Barcelona; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España
Materia
Functional amyloids
Recombinant proteins
Dynamic protein depots
Endocrine-like function
Drug delivery
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/279983
Acceder
id CONICETDig_415dbf994cbde73f0cb669ad73bdf6fe
oai_identifier_str oai:ri.conicet.gov.ar:11336/279983
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Lyophilization of biomimetic amyloids preserves their regulatable, endocrine-like functions for nanoparticle releaseTP Favaro, MariannaLópez Laguna, HèctorVoltà Durán, EricAlba Castellon, LorenaSanchez, Julieta MariaCasanova, IsoldaUnzueta, UgutzMangues, RamónVillaverde, AntonioVázquez, EstherFunctional amyloidsRecombinant proteinsDynamic protein depotsEndocrine-like functionDrug deliveryhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The secretory granules from the mammalian endocrine system are functional amyloids that act as dynamic depots to store and release protein hormones into the bloodstream. The controlled in vitro coordination between divalent cations and solvent-exposed histidine residues triggers reversible, cross-molecular interactions that result in granular protein aggregates with protein-leaking properties. While these synthetic particles are mechanically stable, they progressively disintegrate and release their protein building blocks, mimicking the performance of secretory granules. Envisaged as delivery systems for endocrine-like, time-sustained protein release, their clinical applicability should be supported by robust storage procedures, so far unset. Being lyophilization a desirable storage method for protein drugs, how this procedure could preserve the performance of clinically oriented functional amyloids is a neglected issue. We have here explored, tailored and validated lyophilization as an industrially and clinically friendly, fully scalable approach to the storage of functional amyloids aimed at secretion of protein-only nanoparticles. By doing so, protein-protein interactions in such materials have been characterized, and citrate identified as an efficient modulator of the temporal secretion profile, through which the sustainability of the leaking process can be finely regulated.Fil: TP Favaro, Marianna. Universitat Autònoma de Barcelona; EspañaFil: López Laguna, Hèctor. Universitat Autònoma de Barcelona; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; EspañaFil: Voltà Durán, Eric. Universitat Autònoma de Barcelona; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; EspañaFil: Alba Castellon, Lorena. Institut de Recerca Sant Pau; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España. Josep Carreras Leukaemia Research Institute; EspañaFil: Sanchez, Julieta Maria. 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. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; Argentina. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España. Universitat Autònoma de Barcelona; EspañaFil: Casanova, Isolda. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España. Institut de Recerca Sant Pau; España. Josep Carreras Leukaemia Research Institute; EspañaFil: Unzueta, Ugutz. Josep Carreras Leukaemia Research Institute; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España. Institut de Recerca Sant Pau; EspañaFil: Mangues, Ramón. Josep Carreras Leukaemia Research Institute; España. Institut de Recerca Sant Pau; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; EspañaFil: Villaverde, Antonio. Universitat Autònoma de Barcelona; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; EspañaFil: Vázquez, Esther. Universitat Autònoma de Barcelona; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; EspañaElsevier2024-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/279983TP Favaro, Marianna; López Laguna, Hèctor; Voltà Durán, Eric; Alba Castellon, Lorena; Sanchez, Julieta Maria; et al.; Lyophilization of biomimetic amyloids preserves their regulatable, endocrine-like functions for nanoparticle release; Elsevier; Applied Materials Today; 39; 102348; 8-2024; 1-142352-9407CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S2352940724002932info:eu-repo/semantics/altIdentifier/doi/10.1016/j.apmt.2024.102348info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-02-26T09:58:19Zoai:ri.conicet.gov.ar:11336/279983instacron: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:34982026-02-26 09:58:19.426CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Lyophilization of biomimetic amyloids preserves their regulatable, endocrine-like functions for nanoparticle release
title Lyophilization of biomimetic amyloids preserves their regulatable, endocrine-like functions for nanoparticle release
spellingShingle Lyophilization of biomimetic amyloids preserves their regulatable, endocrine-like functions for nanoparticle release
TP Favaro, Marianna
Functional amyloids
Recombinant proteins
Dynamic protein depots
Endocrine-like function
Drug delivery
title_short Lyophilization of biomimetic amyloids preserves their regulatable, endocrine-like functions for nanoparticle release
title_full Lyophilization of biomimetic amyloids preserves their regulatable, endocrine-like functions for nanoparticle release
title_fullStr Lyophilization of biomimetic amyloids preserves their regulatable, endocrine-like functions for nanoparticle release
title_full_unstemmed Lyophilization of biomimetic amyloids preserves their regulatable, endocrine-like functions for nanoparticle release
title_sort Lyophilization of biomimetic amyloids preserves their regulatable, endocrine-like functions for nanoparticle release
dc.creator.none.fl_str_mv TP Favaro, Marianna
López Laguna, Hèctor
Voltà Durán, Eric
Alba Castellon, Lorena
Sanchez, Julieta Maria
Casanova, Isolda
Unzueta, Ugutz
Mangues, Ramón
Villaverde, Antonio
Vázquez, Esther
author TP Favaro, Marianna
author_facet TP Favaro, Marianna
López Laguna, Hèctor
Voltà Durán, Eric
Alba Castellon, Lorena
Sanchez, Julieta Maria
Casanova, Isolda
Unzueta, Ugutz
Mangues, Ramón
Villaverde, Antonio
Vázquez, Esther
author_role author
author2 López Laguna, Hèctor
Voltà Durán, Eric
Alba Castellon, Lorena
Sanchez, Julieta Maria
Casanova, Isolda
Unzueta, Ugutz
Mangues, Ramón
Villaverde, Antonio
Vázquez, Esther
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Functional amyloids
Recombinant proteins
Dynamic protein depots
Endocrine-like function
Drug delivery
topic Functional amyloids
Recombinant proteins
Dynamic protein depots
Endocrine-like function
Drug delivery
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The secretory granules from the mammalian endocrine system are functional amyloids that act as dynamic depots to store and release protein hormones into the bloodstream. The controlled in vitro coordination between divalent cations and solvent-exposed histidine residues triggers reversible, cross-molecular interactions that result in granular protein aggregates with protein-leaking properties. While these synthetic particles are mechanically stable, they progressively disintegrate and release their protein building blocks, mimicking the performance of secretory granules. Envisaged as delivery systems for endocrine-like, time-sustained protein release, their clinical applicability should be supported by robust storage procedures, so far unset. Being lyophilization a desirable storage method for protein drugs, how this procedure could preserve the performance of clinically oriented functional amyloids is a neglected issue. We have here explored, tailored and validated lyophilization as an industrially and clinically friendly, fully scalable approach to the storage of functional amyloids aimed at secretion of protein-only nanoparticles. By doing so, protein-protein interactions in such materials have been characterized, and citrate identified as an efficient modulator of the temporal secretion profile, through which the sustainability of the leaking process can be finely regulated.
Fil: TP Favaro, Marianna. Universitat Autònoma de Barcelona; España
Fil: López Laguna, Hèctor. Universitat Autònoma de Barcelona; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Voltà Durán, Eric. Universitat Autònoma de Barcelona; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Alba Castellon, Lorena. Institut de Recerca Sant Pau; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España. Josep Carreras Leukaemia Research Institute; España
Fil: Sanchez, Julieta Maria. 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. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; Argentina. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España. Universitat Autònoma de Barcelona; España
Fil: Casanova, Isolda. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España. Institut de Recerca Sant Pau; España. Josep Carreras Leukaemia Research Institute; España
Fil: Unzueta, Ugutz. Josep Carreras Leukaemia Research Institute; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España. Institut de Recerca Sant Pau; España
Fil: Mangues, Ramón. Josep Carreras Leukaemia Research Institute; España. Institut de Recerca Sant Pau; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Villaverde, Antonio. Universitat Autònoma de Barcelona; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Vázquez, Esther. Universitat Autònoma de Barcelona; España. CIBER de Bioingeniería, Biomateriales y Nanomedicina; España
description The secretory granules from the mammalian endocrine system are functional amyloids that act as dynamic depots to store and release protein hormones into the bloodstream. The controlled in vitro coordination between divalent cations and solvent-exposed histidine residues triggers reversible, cross-molecular interactions that result in granular protein aggregates with protein-leaking properties. While these synthetic particles are mechanically stable, they progressively disintegrate and release their protein building blocks, mimicking the performance of secretory granules. Envisaged as delivery systems for endocrine-like, time-sustained protein release, their clinical applicability should be supported by robust storage procedures, so far unset. Being lyophilization a desirable storage method for protein drugs, how this procedure could preserve the performance of clinically oriented functional amyloids is a neglected issue. We have here explored, tailored and validated lyophilization as an industrially and clinically friendly, fully scalable approach to the storage of functional amyloids aimed at secretion of protein-only nanoparticles. By doing so, protein-protein interactions in such materials have been characterized, and citrate identified as an efficient modulator of the temporal secretion profile, through which the sustainability of the leaking process can be finely regulated.
publishDate 2024
dc.date.none.fl_str_mv 2024-08
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/11336/279983
TP Favaro, Marianna; López Laguna, Hèctor; Voltà Durán, Eric; Alba Castellon, Lorena; Sanchez, Julieta Maria; et al.; Lyophilization of biomimetic amyloids preserves their regulatable, endocrine-like functions for nanoparticle release; Elsevier; Applied Materials Today; 39; 102348; 8-2024; 1-14
2352-9407
CONICET Digital
CONICET
url http://hdl.handle.net/11336/279983
identifier_str_mv TP Favaro, Marianna; López Laguna, Hèctor; Voltà Durán, Eric; Alba Castellon, Lorena; Sanchez, Julieta Maria; et al.; Lyophilization of biomimetic amyloids preserves their regulatable, endocrine-like functions for nanoparticle release; Elsevier; Applied Materials Today; 39; 102348; 8-2024; 1-14
2352-9407
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S2352940724002932
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.apmt.2024.102348
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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 13.176822

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