Protein features instruct the secretion dynamics from metal-supported synthetic amyloids

Autores
Parladé, Eloi; Sanchez, Julieta Maria; López Laguna, Héctor; Unzueta, Ugutz; Villaverde, Antonio; Vázquez, Esther
Año de publicación
2023
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Hexahistidine-tagged proteins can be clustered by divalent cations into self-containing, dynamic protein depots at the microscale, which under physiological conditions leak functional protein. While such protein granules show promise in clinics as time-sustained drug delivery systems, little is known about how the nature of their components, that is, the protein and the particular cation used as cross-linker, impact on the disintegration of the material and on its secretory performance. By using four model proteins and four different cation formulations to control aggregation, we have here determined a moderate influence of the used cation and a potent impact of some protein properties on the release kinetics and on the final fraction of releasable protein. In particular, the electrostatic charge at the amino terminus and the instability and hydropathicity indexes determine the disintegration profile of the depot. These data offer clues for the fabrication of efficient and fully exploitable secretory granules that being biocompatible and chemically homogenous allow their tailored use as drug delivery platforms in biological systems.
Fil: Parladé, Eloi. Universitat Autònoma de Barcelona; 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. Universitat Autònoma de Barcelona; España
Fil: López Laguna, Héctor. Universitat Autònoma de Barcelona; España
Fil: Unzueta, Ugutz. Institut d'Investigació Biomèdica Sant Pau; España. Josep Carreras Leukaemia Research Institute; España
Fil: Villaverde, Antonio. Universitat Autònoma de Barcelona; España
Fil: Vázquez, Esther. Universitat Autònoma de Barcelona; España
Materia
Recombinant proteins
Microparticles
Secretory amyloids
Drug delivery system
Time sustained drug release
Building blocks
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/229907
Acceder
id CONICETDig_4551fe7b01ecf324078f91fdf6186447
oai_identifier_str oai:ri.conicet.gov.ar:11336/229907
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Protein features instruct the secretion dynamics from metal-supported synthetic amyloidsParladé, EloiSanchez, Julieta MariaLópez Laguna, HéctorUnzueta, UgutzVillaverde, AntonioVázquez, EstherRecombinant proteinsMicroparticlesSecretory amyloidsDrug delivery systemTime sustained drug releaseBuilding blockshttps://purl.org/becyt/ford/2.10https://purl.org/becyt/ford/2Hexahistidine-tagged proteins can be clustered by divalent cations into self-containing, dynamic protein depots at the microscale, which under physiological conditions leak functional protein. While such protein granules show promise in clinics as time-sustained drug delivery systems, little is known about how the nature of their components, that is, the protein and the particular cation used as cross-linker, impact on the disintegration of the material and on its secretory performance. By using four model proteins and four different cation formulations to control aggregation, we have here determined a moderate influence of the used cation and a potent impact of some protein properties on the release kinetics and on the final fraction of releasable protein. In particular, the electrostatic charge at the amino terminus and the instability and hydropathicity indexes determine the disintegration profile of the depot. These data offer clues for the fabrication of efficient and fully exploitable secretory granules that being biocompatible and chemically homogenous allow their tailored use as drug delivery platforms in biological systems.Fil: Parladé, Eloi. Universitat Autònoma de Barcelona; 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. Universitat Autònoma de Barcelona; EspañaFil: López Laguna, Héctor. Universitat Autònoma de Barcelona; EspañaFil: Unzueta, Ugutz. Institut d'Investigació Biomèdica Sant Pau; España. Josep Carreras Leukaemia Research Institute; EspañaFil: Villaverde, Antonio. Universitat Autònoma de Barcelona; EspañaFil: Vázquez, Esther. Universitat Autònoma de Barcelona; EspañaElsevier Science2023-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/229907Parladé, Eloi; Sanchez, Julieta Maria; López Laguna, Héctor; Unzueta, Ugutz; Villaverde, Antonio; et al.; Protein features instruct the secretion dynamics from metal-supported synthetic amyloids; Elsevier Science; International Journal of Biological Macromolecules; 250; 8-2023; 1-80141-81301879-0003CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S014181302303060Xinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.ijbiomac.2023.126164info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:34:39Zoai:ri.conicet.gov.ar:11336/229907instacron: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 09:34:39.312CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Protein features instruct the secretion dynamics from metal-supported synthetic amyloids
title Protein features instruct the secretion dynamics from metal-supported synthetic amyloids
spellingShingle Protein features instruct the secretion dynamics from metal-supported synthetic amyloids
Parladé, Eloi
Recombinant proteins
Microparticles
Secretory amyloids
Drug delivery system
Time sustained drug release
Building blocks
title_short Protein features instruct the secretion dynamics from metal-supported synthetic amyloids
title_full Protein features instruct the secretion dynamics from metal-supported synthetic amyloids
title_fullStr Protein features instruct the secretion dynamics from metal-supported synthetic amyloids
title_full_unstemmed Protein features instruct the secretion dynamics from metal-supported synthetic amyloids
title_sort Protein features instruct the secretion dynamics from metal-supported synthetic amyloids
dc.creator.none.fl_str_mv Parladé, Eloi
Sanchez, Julieta Maria
López Laguna, Héctor
Unzueta, Ugutz
Villaverde, Antonio
Vázquez, Esther
author Parladé, Eloi
author_facet Parladé, Eloi
Sanchez, Julieta Maria
López Laguna, Héctor
Unzueta, Ugutz
Villaverde, Antonio
Vázquez, Esther
author_role author
author2 Sanchez, Julieta Maria
López Laguna, Héctor
Unzueta, Ugutz
Villaverde, Antonio
Vázquez, Esther
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Recombinant proteins
Microparticles
Secretory amyloids
Drug delivery system
Time sustained drug release
Building blocks
topic Recombinant proteins
Microparticles
Secretory amyloids
Drug delivery system
Time sustained drug release
Building blocks
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.10
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Hexahistidine-tagged proteins can be clustered by divalent cations into self-containing, dynamic protein depots at the microscale, which under physiological conditions leak functional protein. While such protein granules show promise in clinics as time-sustained drug delivery systems, little is known about how the nature of their components, that is, the protein and the particular cation used as cross-linker, impact on the disintegration of the material and on its secretory performance. By using four model proteins and four different cation formulations to control aggregation, we have here determined a moderate influence of the used cation and a potent impact of some protein properties on the release kinetics and on the final fraction of releasable protein. In particular, the electrostatic charge at the amino terminus and the instability and hydropathicity indexes determine the disintegration profile of the depot. These data offer clues for the fabrication of efficient and fully exploitable secretory granules that being biocompatible and chemically homogenous allow their tailored use as drug delivery platforms in biological systems.
Fil: Parladé, Eloi. Universitat Autònoma de Barcelona; 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. Universitat Autònoma de Barcelona; España
Fil: López Laguna, Héctor. Universitat Autònoma de Barcelona; España
Fil: Unzueta, Ugutz. Institut d'Investigació Biomèdica Sant Pau; España. Josep Carreras Leukaemia Research Institute; España
Fil: Villaverde, Antonio. Universitat Autònoma de Barcelona; España
Fil: Vázquez, Esther. Universitat Autònoma de Barcelona; España
description Hexahistidine-tagged proteins can be clustered by divalent cations into self-containing, dynamic protein depots at the microscale, which under physiological conditions leak functional protein. While such protein granules show promise in clinics as time-sustained drug delivery systems, little is known about how the nature of their components, that is, the protein and the particular cation used as cross-linker, impact on the disintegration of the material and on its secretory performance. By using four model proteins and four different cation formulations to control aggregation, we have here determined a moderate influence of the used cation and a potent impact of some protein properties on the release kinetics and on the final fraction of releasable protein. In particular, the electrostatic charge at the amino terminus and the instability and hydropathicity indexes determine the disintegration profile of the depot. These data offer clues for the fabrication of efficient and fully exploitable secretory granules that being biocompatible and chemically homogenous allow their tailored use as drug delivery platforms in biological systems.
publishDate 2023
dc.date.none.fl_str_mv 2023-08
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/11336/229907
Parladé, Eloi; Sanchez, Julieta Maria; López Laguna, Héctor; Unzueta, Ugutz; Villaverde, Antonio; et al.; Protein features instruct the secretion dynamics from metal-supported synthetic amyloids; Elsevier Science; International Journal of Biological Macromolecules; 250; 8-2023; 1-8
0141-8130
1879-0003
CONICET Digital
CONICET
url http://hdl.handle.net/11336/229907
identifier_str_mv Parladé, Eloi; Sanchez, Julieta Maria; López Laguna, Héctor; Unzueta, Ugutz; Villaverde, Antonio; et al.; Protein features instruct the secretion dynamics from metal-supported synthetic amyloids; Elsevier Science; International Journal of Biological Macromolecules; 250; 8-2023; 1-8
0141-8130
1879-0003
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://linkinghub.elsevier.com/retrieve/pii/S014181302303060X
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.ijbiomac.2023.126164
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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_ 1844613073281744896
score 13.070432

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