The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies
- Autores
- Sánchez, Julieta María; Carratalá, José Vicente; Serna, Naroa; Unzueta, Ugutz; Nolan, María Verónica; Sánchez Chardi, Alejandro; Voltà Durán, Eric; López Laguna, Hèctor; Ferrer Miralles, Neus; Villaverde Corrales, Antonio; Vazquez, Esther
- Año de publicación
- 2022
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The coordination between histidine-rich peptides and divalent cations supports the formation of nano-and micro-scale protein biomaterials, including toxic and non-toxic functional amyloids, which can be adapted as drug delivery systems. Among them, inclusion bodies (IBs) formed in recombinant bacteria have shown promise as protein depots for time-sustained protein release. We have demonstrated here that the hexahistidine (H6) tag, fused to recombinant proteins, impacts both on the formation of bacterial IBs and on the conformation of the IB-forming protein, which shows a higher content of cross-beta intermolecular interactions in H6-tagged versions. Additionally, the addition of EDTA during the spontaneous disintegration of isolated IBs largely affects the protein leakage rate, again protein release being stimulated in His-tagged materials. This event depends on the number of His residues but irrespective of the location of the tag in the protein, as it occurs in either C-tagged or N-tagged proteins. The architectonic role of H6 in the formation of bacterial IBs, probably through coordination with divalent cations, offers an easy approach to manipulate protein leakage and to tailor the applicability of this material as a secretory amyloidal depot in different biomedical interfaces. In addition, the findings also offer a model to finely investigate, in a simple set-up, the mechanics of protein release from functional secretory amyloids.
Fil: Sánchez, Julieta María. 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. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Carratalá, José Vicente. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Serna, Naroa. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Unzueta, Ugutz. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Nolan, María Verónica. 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
Fil: Sánchez Chardi, Alejandro. Universidad de Barcelona; España. Universitat Autònoma de Barcelona; España
Fil: Voltà Durán, Eric. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: López Laguna, Hèctor. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Ferrer Miralles, Neus. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Villaverde Corrales, Antonio. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España
Fil: Vazquez, Esther. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España - Materia
-
INCLUSION BODIES
FUNCTIONAL AMYLOIDS
PROTEIN SECRETION
HIS–CATION COORDINATION
BIOMATERIALS
PROTEIN MATERIALS
SLOW PROTEIN RELEASE
DRUG DELIVERY - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/167038
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The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion BodiesSánchez, Julieta MaríaCarratalá, José VicenteSerna, NaroaUnzueta, UgutzNolan, María VerónicaSánchez Chardi, AlejandroVoltà Durán, EricLópez Laguna, HèctorFerrer Miralles, NeusVillaverde Corrales, AntonioVazquez, EstherINCLUSION BODIESFUNCTIONAL AMYLOIDSPROTEIN SECRETIONHIS–CATION COORDINATIONBIOMATERIALSPROTEIN MATERIALSSLOW PROTEIN RELEASEDRUG DELIVERYhttps://purl.org/becyt/ford/2.10https://purl.org/becyt/ford/2The coordination between histidine-rich peptides and divalent cations supports the formation of nano-and micro-scale protein biomaterials, including toxic and non-toxic functional amyloids, which can be adapted as drug delivery systems. Among them, inclusion bodies (IBs) formed in recombinant bacteria have shown promise as protein depots for time-sustained protein release. We have demonstrated here that the hexahistidine (H6) tag, fused to recombinant proteins, impacts both on the formation of bacterial IBs and on the conformation of the IB-forming protein, which shows a higher content of cross-beta intermolecular interactions in H6-tagged versions. Additionally, the addition of EDTA during the spontaneous disintegration of isolated IBs largely affects the protein leakage rate, again protein release being stimulated in His-tagged materials. This event depends on the number of His residues but irrespective of the location of the tag in the protein, as it occurs in either C-tagged or N-tagged proteins. The architectonic role of H6 in the formation of bacterial IBs, probably through coordination with divalent cations, offers an easy approach to manipulate protein leakage and to tailor the applicability of this material as a secretory amyloidal depot in different biomedical interfaces. In addition, the findings also offer a model to finely investigate, in a simple set-up, the mechanics of protein release from functional secretory amyloids.Fil: Sánchez, Julieta María. 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. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; EspañaFil: Carratalá, José Vicente. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; EspañaFil: Serna, Naroa. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; EspañaFil: Unzueta, Ugutz. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; EspañaFil: Nolan, María Verónica. 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; ArgentinaFil: Sánchez Chardi, Alejandro. Universidad de Barcelona; España. Universitat Autònoma de Barcelona; EspañaFil: Voltà Durán, Eric. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; EspañaFil: López Laguna, Hèctor. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; EspañaFil: Ferrer Miralles, Neus. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; EspañaFil: Villaverde Corrales, Antonio. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; EspañaFil: Vazquez, Esther. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; EspañaMultidisciplinary Digital Publishing Institute2022-03-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/167038Sánchez, Julieta María; Carratalá, José Vicente; Serna, Naroa; Unzueta, Ugutz; Nolan, María Verónica; et al.; The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies; Multidisciplinary Digital Publishing Institute; Pharmaceutics; 14; 3; 10-3-2022; 1-121999-4923CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/1999-4923/14/3/602info:eu-repo/semantics/altIdentifier/doi/10.3390/pharmaceutics14030602info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:13:33Zoai:ri.conicet.gov.ar:11336/167038instacron: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 10:13:33.233CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies |
title |
The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies |
spellingShingle |
The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies Sánchez, Julieta María INCLUSION BODIES FUNCTIONAL AMYLOIDS PROTEIN SECRETION HIS–CATION COORDINATION BIOMATERIALS PROTEIN MATERIALS SLOW PROTEIN RELEASE DRUG DELIVERY |
title_short |
The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies |
title_full |
The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies |
title_fullStr |
The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies |
title_full_unstemmed |
The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies |
title_sort |
The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies |
dc.creator.none.fl_str_mv |
Sánchez, Julieta María Carratalá, José Vicente Serna, Naroa Unzueta, Ugutz Nolan, María Verónica Sánchez Chardi, Alejandro Voltà Durán, Eric López Laguna, Hèctor Ferrer Miralles, Neus Villaverde Corrales, Antonio Vazquez, Esther |
author |
Sánchez, Julieta María |
author_facet |
Sánchez, Julieta María Carratalá, José Vicente Serna, Naroa Unzueta, Ugutz Nolan, María Verónica Sánchez Chardi, Alejandro Voltà Durán, Eric López Laguna, Hèctor Ferrer Miralles, Neus Villaverde Corrales, Antonio Vazquez, Esther |
author_role |
author |
author2 |
Carratalá, José Vicente Serna, Naroa Unzueta, Ugutz Nolan, María Verónica Sánchez Chardi, Alejandro Voltà Durán, Eric López Laguna, Hèctor Ferrer Miralles, Neus Villaverde Corrales, Antonio Vazquez, Esther |
author2_role |
author author author author author author author author author author |
dc.subject.none.fl_str_mv |
INCLUSION BODIES FUNCTIONAL AMYLOIDS PROTEIN SECRETION HIS–CATION COORDINATION BIOMATERIALS PROTEIN MATERIALS SLOW PROTEIN RELEASE DRUG DELIVERY |
topic |
INCLUSION BODIES FUNCTIONAL AMYLOIDS PROTEIN SECRETION HIS–CATION COORDINATION BIOMATERIALS PROTEIN MATERIALS SLOW PROTEIN RELEASE DRUG DELIVERY |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.10 https://purl.org/becyt/ford/2 |
dc.description.none.fl_txt_mv |
The coordination between histidine-rich peptides and divalent cations supports the formation of nano-and micro-scale protein biomaterials, including toxic and non-toxic functional amyloids, which can be adapted as drug delivery systems. Among them, inclusion bodies (IBs) formed in recombinant bacteria have shown promise as protein depots for time-sustained protein release. We have demonstrated here that the hexahistidine (H6) tag, fused to recombinant proteins, impacts both on the formation of bacterial IBs and on the conformation of the IB-forming protein, which shows a higher content of cross-beta intermolecular interactions in H6-tagged versions. Additionally, the addition of EDTA during the spontaneous disintegration of isolated IBs largely affects the protein leakage rate, again protein release being stimulated in His-tagged materials. This event depends on the number of His residues but irrespective of the location of the tag in the protein, as it occurs in either C-tagged or N-tagged proteins. The architectonic role of H6 in the formation of bacterial IBs, probably through coordination with divalent cations, offers an easy approach to manipulate protein leakage and to tailor the applicability of this material as a secretory amyloidal depot in different biomedical interfaces. In addition, the findings also offer a model to finely investigate, in a simple set-up, the mechanics of protein release from functional secretory amyloids. Fil: Sánchez, Julieta María. 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. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España Fil: Carratalá, José Vicente. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España Fil: Serna, Naroa. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España Fil: Unzueta, Ugutz. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España Fil: Nolan, María Verónica. 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 Fil: Sánchez Chardi, Alejandro. Universidad de Barcelona; España. Universitat Autònoma de Barcelona; España Fil: Voltà Durán, Eric. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España Fil: López Laguna, Hèctor. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España Fil: Ferrer Miralles, Neus. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España Fil: Villaverde Corrales, Antonio. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España Fil: Vazquez, Esther. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España |
description |
The coordination between histidine-rich peptides and divalent cations supports the formation of nano-and micro-scale protein biomaterials, including toxic and non-toxic functional amyloids, which can be adapted as drug delivery systems. Among them, inclusion bodies (IBs) formed in recombinant bacteria have shown promise as protein depots for time-sustained protein release. We have demonstrated here that the hexahistidine (H6) tag, fused to recombinant proteins, impacts both on the formation of bacterial IBs and on the conformation of the IB-forming protein, which shows a higher content of cross-beta intermolecular interactions in H6-tagged versions. Additionally, the addition of EDTA during the spontaneous disintegration of isolated IBs largely affects the protein leakage rate, again protein release being stimulated in His-tagged materials. This event depends on the number of His residues but irrespective of the location of the tag in the protein, as it occurs in either C-tagged or N-tagged proteins. The architectonic role of H6 in the formation of bacterial IBs, probably through coordination with divalent cations, offers an easy approach to manipulate protein leakage and to tailor the applicability of this material as a secretory amyloidal depot in different biomedical interfaces. In addition, the findings also offer a model to finely investigate, in a simple set-up, the mechanics of protein release from functional secretory amyloids. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-03-10 |
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/11336/167038 Sánchez, Julieta María; Carratalá, José Vicente; Serna, Naroa; Unzueta, Ugutz; Nolan, María Verónica; et al.; The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies; Multidisciplinary Digital Publishing Institute; Pharmaceutics; 14; 3; 10-3-2022; 1-12 1999-4923 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/167038 |
identifier_str_mv |
Sánchez, Julieta María; Carratalá, José Vicente; Serna, Naroa; Unzueta, Ugutz; Nolan, María Verónica; et al.; The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies; Multidisciplinary Digital Publishing Institute; Pharmaceutics; 14; 3; 10-3-2022; 1-12 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/url/https://www.mdpi.com/1999-4923/14/3/602 info:eu-repo/semantics/altIdentifier/doi/10.3390/pharmaceutics14030602 |
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 |
publisher.none.fl_str_mv |
Multidisciplinary Digital Publishing Institute |
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) |
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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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1844614052946378752 |
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13.070432 |