Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids

Autores
Sanchez, Julieta Maria; López Laguna, Hèctor; Parladé, Eloi; Somma, Angela Di; Livieri, Andrea L.; Álamo, Patricia; Mangues, Ramón; Unzueta, Ugutz; Villaverde, Antonio; Vázquez, Esther
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Developing time-sustained drug delivery systems is a main goal in innovative medicines. Inspired by the architecture of secretory granules from the mammalian endocrine system it has generated non-toxic microscale amyloid materials through the coordination between divalent metals and poly-histidine stretches. Like their natural counterparts that keep the functionalities of the assembled protein, those synthetic structures release biologically active proteins during a slow self-disintegration process occurring in vitro and upon in vivo administration. Being these granules formed by a single pure protein species and therefore, chemically homogenous, they act as highly promising time-sustained drug delivery systems. Despite their enormous clinical potential, the nature of the clustering process and the quality of the released protein have been so far neglected issues. By using diverse polypeptide species and their protein-only oligomeric nanoscale versions as convenient models, a conformational rearrangement and a stabilization of the building blocks during their transit through the secretory granules, being the released material structurally distinguishable from the original source is proved here. This fact indicates a dynamic nature of secretory amyloids that act as conformational arrangers rather than as plain, inert protein-recruiting/protein-releasing granular depots.
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. Universitat Autònoma de Barcelona; España
Fil: López Laguna, Hèctor. Universitat Autònoma de Barcelona; España
Fil: Parladé, Eloi. Universitat Autònoma de Barcelona; España
Fil: Somma, Angela Di. Universitat Autònoma de Barcelona; España
Fil: Livieri, Andrea L.. Universitat Autònoma de Barcelona; España
Fil: Álamo, Patricia. Hospital de la Santa Creu I Sant Pau; España
Fil: Mangues, Ramón. Hospital de la Santa Creu I Sant Pau; España
Fil: Unzueta, Ugutz. Universitat Autònoma de Barcelona; España
Fil: Villaverde, Antonio. Universitat Autònoma de Barcelona; España
Fil: Vázquez, Esther. Universitat Autònoma de Barcelona; España
Materia
Cell-targeting
Drug delivery
Microparticles
Nanoparticles
Recombinant proteins
Secretory granules
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:11336/242116
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/242116
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory AmyloidsSanchez, Julieta MariaLópez Laguna, HèctorParladé, EloiSomma, Angela DiLivieri, Andrea L.Álamo, PatriciaMangues, RamónUnzueta, UgutzVillaverde, AntonioVázquez, EstherCell-targetingDrug deliveryMicroparticlesNanoparticlesRecombinant proteinsSecretory granuleshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Developing time-sustained drug delivery systems is a main goal in innovative medicines. Inspired by the architecture of secretory granules from the mammalian endocrine system it has generated non-toxic microscale amyloid materials through the coordination between divalent metals and poly-histidine stretches. Like their natural counterparts that keep the functionalities of the assembled protein, those synthetic structures release biologically active proteins during a slow self-disintegration process occurring in vitro and upon in vivo administration. Being these granules formed by a single pure protein species and therefore, chemically homogenous, they act as highly promising time-sustained drug delivery systems. Despite their enormous clinical potential, the nature of the clustering process and the quality of the released protein have been so far neglected issues. By using diverse polypeptide species and their protein-only oligomeric nanoscale versions as convenient models, a conformational rearrangement and a stabilization of the building blocks during their transit through the secretory granules, being the released material structurally distinguishable from the original source is proved here. This fact indicates a dynamic nature of secretory amyloids that act as conformational arrangers rather than as plain, inert protein-recruiting/protein-releasing granular depots.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. Universitat Autònoma de Barcelona; EspañaFil: López Laguna, Hèctor. Universitat Autònoma de Barcelona; EspañaFil: Parladé, Eloi. Universitat Autònoma de Barcelona; EspañaFil: Somma, Angela Di. Universitat Autònoma de Barcelona; EspañaFil: Livieri, Andrea L.. Universitat Autònoma de Barcelona; EspañaFil: Álamo, Patricia. Hospital de la Santa Creu I Sant Pau; EspañaFil: Mangues, Ramón. Hospital de la Santa Creu I Sant Pau; EspañaFil: Unzueta, Ugutz. Universitat Autònoma de Barcelona; EspañaFil: Villaverde, Antonio. Universitat Autònoma de Barcelona; EspañaFil: Vázquez, Esther. Universitat Autònoma de Barcelona; EspañaWiley2024-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/242116Sanchez, Julieta Maria; López Laguna, Hèctor; Parladé, Eloi; Somma, Angela Di; Livieri, Andrea L.; et al.; Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids; Wiley; Advanced Science; 11; 21; 3-2024; 1-112198-3844CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1002/advs.202309427info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1002/advs.202309427info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:49:16Zoai:ri.conicet.gov.ar:11336/242116instacron: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:34982025-09-03 09:49:16.851CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids
title Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids
spellingShingle Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids
Sanchez, Julieta Maria
Cell-targeting
Drug delivery
Microparticles
Nanoparticles
Recombinant proteins
Secretory granules
title_short Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids
title_full Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids
title_fullStr Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids
title_full_unstemmed Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids
title_sort Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids
dc.creator.none.fl_str_mv Sanchez, Julieta Maria
López Laguna, Hèctor
Parladé, Eloi
Somma, Angela Di
Livieri, Andrea L.
Álamo, Patricia
Mangues, Ramón
Unzueta, Ugutz
Villaverde, Antonio
Vázquez, Esther
author Sanchez, Julieta Maria
author_facet Sanchez, Julieta Maria
López Laguna, Hèctor
Parladé, Eloi
Somma, Angela Di
Livieri, Andrea L.
Álamo, Patricia
Mangues, Ramón
Unzueta, Ugutz
Villaverde, Antonio
Vázquez, Esther
author_role author
author2 López Laguna, Hèctor
Parladé, Eloi
Somma, Angela Di
Livieri, Andrea L.
Álamo, Patricia
Mangues, Ramón
Unzueta, Ugutz
Villaverde, Antonio
Vázquez, Esther
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Cell-targeting
Drug delivery
Microparticles
Nanoparticles
Recombinant proteins
Secretory granules
topic Cell-targeting
Drug delivery
Microparticles
Nanoparticles
Recombinant proteins
Secretory granules
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Developing time-sustained drug delivery systems is a main goal in innovative medicines. Inspired by the architecture of secretory granules from the mammalian endocrine system it has generated non-toxic microscale amyloid materials through the coordination between divalent metals and poly-histidine stretches. Like their natural counterparts that keep the functionalities of the assembled protein, those synthetic structures release biologically active proteins during a slow self-disintegration process occurring in vitro and upon in vivo administration. Being these granules formed by a single pure protein species and therefore, chemically homogenous, they act as highly promising time-sustained drug delivery systems. Despite their enormous clinical potential, the nature of the clustering process and the quality of the released protein have been so far neglected issues. By using diverse polypeptide species and their protein-only oligomeric nanoscale versions as convenient models, a conformational rearrangement and a stabilization of the building blocks during their transit through the secretory granules, being the released material structurally distinguishable from the original source is proved here. This fact indicates a dynamic nature of secretory amyloids that act as conformational arrangers rather than as plain, inert protein-recruiting/protein-releasing granular depots.
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. Universitat Autònoma de Barcelona; España
Fil: López Laguna, Hèctor. Universitat Autònoma de Barcelona; España
Fil: Parladé, Eloi. Universitat Autònoma de Barcelona; España
Fil: Somma, Angela Di. Universitat Autònoma de Barcelona; España
Fil: Livieri, Andrea L.. Universitat Autònoma de Barcelona; España
Fil: Álamo, Patricia. Hospital de la Santa Creu I Sant Pau; España
Fil: Mangues, Ramón. Hospital de la Santa Creu I Sant Pau; España
Fil: Unzueta, Ugutz. Universitat Autònoma de Barcelona; España
Fil: Villaverde, Antonio. Universitat Autònoma de Barcelona; España
Fil: Vázquez, Esther. Universitat Autònoma de Barcelona; España
description Developing time-sustained drug delivery systems is a main goal in innovative medicines. Inspired by the architecture of secretory granules from the mammalian endocrine system it has generated non-toxic microscale amyloid materials through the coordination between divalent metals and poly-histidine stretches. Like their natural counterparts that keep the functionalities of the assembled protein, those synthetic structures release biologically active proteins during a slow self-disintegration process occurring in vitro and upon in vivo administration. Being these granules formed by a single pure protein species and therefore, chemically homogenous, they act as highly promising time-sustained drug delivery systems. Despite their enormous clinical potential, the nature of the clustering process and the quality of the released protein have been so far neglected issues. By using diverse polypeptide species and their protein-only oligomeric nanoscale versions as convenient models, a conformational rearrangement and a stabilization of the building blocks during their transit through the secretory granules, being the released material structurally distinguishable from the original source is proved here. This fact indicates a dynamic nature of secretory amyloids that act as conformational arrangers rather than as plain, inert protein-recruiting/protein-releasing granular depots.
publishDate 2024
dc.date.none.fl_str_mv 2024-03
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/11336/242116
Sanchez, Julieta Maria; López Laguna, Hèctor; Parladé, Eloi; Somma, Angela Di; Livieri, Andrea L.; et al.; Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids; Wiley; Advanced Science; 11; 21; 3-2024; 1-11
2198-3844
CONICET Digital
CONICET
url http://hdl.handle.net/11336/242116
identifier_str_mv Sanchez, Julieta Maria; López Laguna, Hèctor; Parladé, Eloi; Somma, Angela Di; Livieri, Andrea L.; et al.; Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids; Wiley; Advanced Science; 11; 21; 3-2024; 1-11
2198-3844
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1002/advs.202309427
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1002/advs.202309427
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 Wiley
publisher.none.fl_str_mv Wiley
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
_version_ 1842268964332240896
score 13.13397

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