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

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 know...

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Authors: Parladé E., Sánchez J.M., López-Laguna H., Unzueta U., Villaverde A., Vázquez E.
Format: article
Status:Published version
Publication Date:2023
Country:España
Institution:Institut d’Investigació Biomèdica Sant Pau (IIB Sant Pau)
Repository:r-IIB SANT PAU. Repositorio Institucional de Producción Científica del Instituto de Investigación Biomédica Sant Pau
OAI Identifier:oai:iibsantpau.fundanetsuite.com:p16655
Online Access:https://iibsantpau.fundanetsuite.com/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=16655
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85167421589&doi=10.1016%2fj.ijbiomac.2023.126164&partnerID=40&md5=7bdd04aec22048be6908dfcfa7b6809b
Access Level:Open access
Keyword:Building blocks
Drug delivery system
Microparticles
Recombinant proteins
Secretory amyloids
Time sustained drug release
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spelling Protein features instruct the secretion dynamics from metal-supported synthetic amyloidsParladé E.Sánchez J.M.López-Laguna H.Unzueta U.Villaverde A.Vázquez E.Building blocksDrug delivery systemMicroparticlesRecombinant proteinsSecretory amyloidsTime sustained drug releaseHexahistidine-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.Elsevier B.V.2023info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttps://iibsantpau.fundanetsuite.com/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=16655https://www.scopus.com/inward/record.uri?eid=2-s2.0-85167421589&doi=10.1016%2fj.ijbiomac.2023.126164&partnerID=40&md5=7bdd04aec22048be6908dfcfa7b6809bINTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULESISSN: 01418130ISSNe: 18790003reponame:r-IIB SANT PAU. Repositorio Institucional de Producción Científica del Instituto de Investigación Biomédica Sant Pauinstname:Institut d’Investigació Biomèdica Sant Pau (IIB Sant Pau)Inglésinfo:eu-repo/semantics/openAccessoai:iibsantpau.fundanetsuite.com:p166552026-06-14T12:41:47Z
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 E.
Building blocks
Drug delivery system
Microparticles
Recombinant proteins
Secretory amyloids
Time sustained drug release
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 E.
Sánchez J.M.
López-Laguna H.
Unzueta U.
Villaverde A.
Vázquez E.
author Parladé E.
author_facet Parladé E.
Sánchez J.M.
López-Laguna H.
Unzueta U.
Villaverde A.
Vázquez E.
author_role author
author2 Sánchez J.M.
López-Laguna H.
Unzueta U.
Villaverde A.
Vázquez E.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Building blocks
Drug delivery system
Microparticles
Recombinant proteins
Secretory amyloids
Time sustained drug release
topic Building blocks
Drug delivery system
Microparticles
Recombinant proteins
Secretory amyloids
Time sustained drug release
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
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://iibsantpau.fundanetsuite.com/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=16655
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85167421589&doi=10.1016%2fj.ijbiomac.2023.126164&partnerID=40&md5=7bdd04aec22048be6908dfcfa7b6809b
url https://iibsantpau.fundanetsuite.com/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=16655
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85167421589&doi=10.1016%2fj.ijbiomac.2023.126164&partnerID=40&md5=7bdd04aec22048be6908dfcfa7b6809b
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier B.V.
publisher.none.fl_str_mv Elsevier B.V.
dc.source.none.fl_str_mv INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
ISSN: 01418130
ISSNe: 18790003
reponame:r-IIB SANT PAU. Repositorio Institucional de Producción Científica del Instituto de Investigación Biomédica Sant Pau
instname:Institut d’Investigació Biomèdica Sant Pau (IIB Sant Pau)
instname_str Institut d’Investigació Biomèdica Sant Pau (IIB Sant Pau)
reponame_str r-IIB SANT PAU. Repositorio Institucional de Producción Científica del Instituto de Investigación Biomédica Sant Pau
collection r-IIB SANT PAU. Repositorio Institucional de Producción Científica del Instituto de Investigación Biomédica Sant Pau
repository.name.fl_str_mv
repository.mail.fl_str_mv
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