Surpassing protein specificity in biomimetics of bacterial amyloids

In nature, nontoxic protein amyloids serve as dynamic, protein-specific depots, exemplified by both bacterial inclusion bodies and secretory granules from the endocrine system. Inspired by these systems, chemically defined and regulatory-compliant artificial protein microgranules have been developed...

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Autores: Sánchez, Julieta M.|||0000-0001-6676-5776, Voltà-Durán, Eric|||0000-0003-0017-8274, Parladé Molist, Eloi|||0000-0001-5750-550X, Mangues, Ramon|||0000-0003-2661-9525, Villaverde, Antonio|||0000-0002-2615-4521, Vázquez, Esther|||0000-0003-1052-0424, Unzueta Elorza, Ugutz|||0000-0001-5119-2266
Tipo de recurso: artículo
Fecha de publicación:2025
País:España
Institución:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:308371
Acceso en línea:https://ddd.uab.cat/record/308371
https://dx.doi.org/urn:doi:10.1016/j.ijbiomac.2025.139635
Access Level:acceso abierto
Palabra clave:Recombinant protein
Microparticles
Amyloids
Biomimetics
Protein materials
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spelling Surpassing protein specificity in biomimetics of bacterial amyloidsSánchez, Julieta M.|||0000-0001-6676-5776Voltà-Durán, Eric|||0000-0003-0017-8274Parladé Molist, Eloi|||0000-0001-5750-550XMangues, Ramon|||0000-0003-2661-9525Villaverde, Antonio|||0000-0002-2615-4521Vázquez, Esther|||0000-0003-1052-0424Unzueta Elorza, Ugutz|||0000-0001-5119-2266Recombinant proteinMicroparticlesAmyloidsBiomimeticsProtein materialsIn nature, nontoxic protein amyloids serve as dynamic, protein-specific depots, exemplified by both bacterial inclusion bodies and secretory granules from the endocrine system. Inspired by these systems, chemically defined and regulatory-compliant artificial protein microgranules have been developed for clinical applications as endocrine-like protein repositories. This has been achieved by exploiting the reversible coordination between histidine residues and divalent cations such as Zn, that promotes protein-protein interactions. While stereospecificity is a main architectonic feature of natural amyloids, the potential for synthetic approaches to create hybrid protein materials remains unexplored. Such materials could enable the occurrence and synchronized local application of diverse proteins in predefined molar ratios, for coupled enzymatic reactions or delivery of synergistically acting polypeptides. Here, we report on the fabrication of artificial protein granules with amyloidal architecture formed by combining two structurally distinct polypeptides. Specifically, we tested co-aggregation of the pairs GFP/IRFP and GFP/β-galactosidase. The formation of hybrid microparticles was confirmed through FRET and complementary methodologies, demonstrating that the His-Zn clustering technology does not require sequential or structural homologies between aggregating polypeptides. This approach opens new avenues for the development of functional depots that capitalize on synergistic protein functionalities, paving the way for next-generation functional materials. 22025-01-0120252025-01-01Articlehttp://purl.org/coar/resource_type/c_6501AMhttp://purl.org/coar/version/c_ab4af688f83e57aainfo:eu-repo/semantics/articleapplication/pdfhttps://ddd.uab.cat/record/308371https://dx.doi.org/urn:doi:10.1016/j.ijbiomac.2025.139635reponame:Dipòsit Digital de Documents de la UABinstname:Universitat Autònoma de BarcelonaInglésengAgencia Estatal de Investigación https://doi.org/10.13039/501100011033 PDC2022-133858-I00Agencia Estatal de Investigación https://doi.org/10.13039/501100011033 PID2022-1368450Agencia Estatal de Investigación https://doi.org/10.13039/501100011033 PID2019-105416RB-I00Ministerio de Sanidad y Consumo CB06/01/0014Ministerio de Sanidad y Consumo CB06/01/1031Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 PI23/00318Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 PI20/00400Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 CP19/00028Agència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2021/SGR-00092open accesshttp://purl.org/coar/access_right/c_abf2Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, i la comunicació pública de l'obra, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original. No es permet la creació d'obres derivades.https://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:ddd.uab.cat:3083712026-06-06T12:50:31Z
dc.title.none.fl_str_mv Surpassing protein specificity in biomimetics of bacterial amyloids
title Surpassing protein specificity in biomimetics of bacterial amyloids
spellingShingle Surpassing protein specificity in biomimetics of bacterial amyloids
Sánchez, Julieta M.|||0000-0001-6676-5776
Recombinant protein
Microparticles
Amyloids
Biomimetics
Protein materials
title_short Surpassing protein specificity in biomimetics of bacterial amyloids
title_full Surpassing protein specificity in biomimetics of bacterial amyloids
title_fullStr Surpassing protein specificity in biomimetics of bacterial amyloids
title_full_unstemmed Surpassing protein specificity in biomimetics of bacterial amyloids
title_sort Surpassing protein specificity in biomimetics of bacterial amyloids
dc.creator.none.fl_str_mv Sánchez, Julieta M.|||0000-0001-6676-5776
Voltà-Durán, Eric|||0000-0003-0017-8274
Parladé Molist, Eloi|||0000-0001-5750-550X
Mangues, Ramon|||0000-0003-2661-9525
Villaverde, Antonio|||0000-0002-2615-4521
Vázquez, Esther|||0000-0003-1052-0424
Unzueta Elorza, Ugutz|||0000-0001-5119-2266
author Sánchez, Julieta M.|||0000-0001-6676-5776
author_facet Sánchez, Julieta M.|||0000-0001-6676-5776
Voltà-Durán, Eric|||0000-0003-0017-8274
Parladé Molist, Eloi|||0000-0001-5750-550X
Mangues, Ramon|||0000-0003-2661-9525
Villaverde, Antonio|||0000-0002-2615-4521
Vázquez, Esther|||0000-0003-1052-0424
Unzueta Elorza, Ugutz|||0000-0001-5119-2266
author_role author
author2 Voltà-Durán, Eric|||0000-0003-0017-8274
Parladé Molist, Eloi|||0000-0001-5750-550X
Mangues, Ramon|||0000-0003-2661-9525
Villaverde, Antonio|||0000-0002-2615-4521
Vázquez, Esther|||0000-0003-1052-0424
Unzueta Elorza, Ugutz|||0000-0001-5119-2266
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Recombinant protein
Microparticles
Amyloids
Biomimetics
Protein materials
topic Recombinant protein
Microparticles
Amyloids
Biomimetics
Protein materials
description In nature, nontoxic protein amyloids serve as dynamic, protein-specific depots, exemplified by both bacterial inclusion bodies and secretory granules from the endocrine system. Inspired by these systems, chemically defined and regulatory-compliant artificial protein microgranules have been developed for clinical applications as endocrine-like protein repositories. This has been achieved by exploiting the reversible coordination between histidine residues and divalent cations such as Zn, that promotes protein-protein interactions. While stereospecificity is a main architectonic feature of natural amyloids, the potential for synthetic approaches to create hybrid protein materials remains unexplored. Such materials could enable the occurrence and synchronized local application of diverse proteins in predefined molar ratios, for coupled enzymatic reactions or delivery of synergistically acting polypeptides. Here, we report on the fabrication of artificial protein granules with amyloidal architecture formed by combining two structurally distinct polypeptides. Specifically, we tested co-aggregation of the pairs GFP/IRFP and GFP/β-galactosidase. The formation of hybrid microparticles was confirmed through FRET and complementary methodologies, demonstrating that the His-Zn clustering technology does not require sequential or structural homologies between aggregating polypeptides. This approach opens new avenues for the development of functional depots that capitalize on synergistic protein functionalities, paving the way for next-generation functional materials.
publishDate 2025
dc.date.none.fl_str_mv 2
2025-01-01
2025
2025-01-01
dc.type.none.fl_str_mv Article
http://purl.org/coar/resource_type/c_6501
AM
http://purl.org/coar/version/c_ab4af688f83e57aa
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://ddd.uab.cat/record/308371
https://dx.doi.org/urn:doi:10.1016/j.ijbiomac.2025.139635
url https://ddd.uab.cat/record/308371
https://dx.doi.org/urn:doi:10.1016/j.ijbiomac.2025.139635
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv Agencia Estatal de Investigación https://doi.org/10.13039/501100011033 PDC2022-133858-I00
Agencia Estatal de Investigación https://doi.org/10.13039/501100011033 PID2022-1368450
Agencia Estatal de Investigación https://doi.org/10.13039/501100011033 PID2019-105416RB-I00
Ministerio de Sanidad y Consumo CB06/01/0014
Ministerio de Sanidad y Consumo CB06/01/1031
Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 PI23/00318
Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 PI20/00400
Instituto de Salud Carlos III https://doi.org/10.13039/501100004587 CP19/00028
Agència de Gestió d'Ajuts Universitaris i de Recerca https://doi.org/10.13039/501100003030 2021/SGR-00092
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Dipòsit Digital de Documents de la UAB
instname:Universitat Autònoma de Barcelona
instname_str Universitat Autònoma de Barcelona
reponame_str Dipòsit Digital de Documents de la UAB
collection Dipòsit Digital de Documents de la UAB
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repository.mail.fl_str_mv
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