Size-tunable LDH-protein hybrids towards the optimization of drug nanocarriers

Autores
Rojas Delgado, Ricardo; Giacomelli, Carla Eugenia
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Layered double hydroxides (LDHs) are extensively investigated as drug nanocarriers due to their anion exchange properties and potential capacity to achieve enhanced cellular trafficking and targeted delivery. In this work, LDH–protein hybrids with controlled particle size were obtained by modulation of the charge and hydrophobicity of LDH matrixes. In order to do that, bovine serum albumin (BSA) adsorption was studied in LDH matrixes intercalated with chloride and dodecylsulfate (DS−) in different ratios and its dependence on pH and ionic strength was determined. Positively charged LDH-Cl matrixes in aqueous solution changed from micro- to nano-size when adsorbing BSA molecules at pH values higher than the isoelectric point of the protein. On the other hand, the low BSA hybridization with a negatively charged LDH-DS matrix was not enough to reduce its particle size. However, a fine tuning of the physicochemical properties of the LDH-Cl matrix by controlled DS− incorporation and pH and ionic strength conditions allowed LDH–BSA nanohybrids to be partially intercalated with the surfactant that exhibited colloidal stability at high ionic strength (similar to that of biological fluids).
Fil: Rojas Delgado, Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
Fil: Giacomelli, Carla Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
Materia
Nanohybrids
Electrostatic Interactions
Steric Repulsion
Interfacial Modification
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/47135

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spelling Size-tunable LDH-protein hybrids towards the optimization of drug nanocarriersRojas Delgado, RicardoGiacomelli, Carla EugeniaNanohybridsElectrostatic InteractionsSteric RepulsionInterfacial Modificationhttps://purl.org/becyt/ford/2.10https://purl.org/becyt/ford/2Layered double hydroxides (LDHs) are extensively investigated as drug nanocarriers due to their anion exchange properties and potential capacity to achieve enhanced cellular trafficking and targeted delivery. In this work, LDH–protein hybrids with controlled particle size were obtained by modulation of the charge and hydrophobicity of LDH matrixes. In order to do that, bovine serum albumin (BSA) adsorption was studied in LDH matrixes intercalated with chloride and dodecylsulfate (DS−) in different ratios and its dependence on pH and ionic strength was determined. Positively charged LDH-Cl matrixes in aqueous solution changed from micro- to nano-size when adsorbing BSA molecules at pH values higher than the isoelectric point of the protein. On the other hand, the low BSA hybridization with a negatively charged LDH-DS matrix was not enough to reduce its particle size. However, a fine tuning of the physicochemical properties of the LDH-Cl matrix by controlled DS− incorporation and pH and ionic strength conditions allowed LDH–BSA nanohybrids to be partially intercalated with the surfactant that exhibited colloidal stability at high ionic strength (similar to that of biological fluids).Fil: Rojas Delgado, Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; ArgentinaFil: Giacomelli, Carla Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; ArgentinaRoyal Society of Chemistry2015-02-18info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/47135Rojas Delgado, Ricardo; Giacomelli, Carla Eugenia; Size-tunable LDH-protein hybrids towards the optimization of drug nanocarriers; Royal Society of Chemistry; Journal of Materials Chemistry B; 3; 14; 18-2-2015; 2778-27852050-750X2050-7518CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2015/TB/C4TB01992J#info:eu-repo/semantics/altIdentifier/doi/10.1039/c4tb01992jinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:39:43Zoai:ri.conicet.gov.ar:11336/47135instacron: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 10:39:43.848CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Size-tunable LDH-protein hybrids towards the optimization of drug nanocarriers
title Size-tunable LDH-protein hybrids towards the optimization of drug nanocarriers
spellingShingle Size-tunable LDH-protein hybrids towards the optimization of drug nanocarriers
Rojas Delgado, Ricardo
Nanohybrids
Electrostatic Interactions
Steric Repulsion
Interfacial Modification
title_short Size-tunable LDH-protein hybrids towards the optimization of drug nanocarriers
title_full Size-tunable LDH-protein hybrids towards the optimization of drug nanocarriers
title_fullStr Size-tunable LDH-protein hybrids towards the optimization of drug nanocarriers
title_full_unstemmed Size-tunable LDH-protein hybrids towards the optimization of drug nanocarriers
title_sort Size-tunable LDH-protein hybrids towards the optimization of drug nanocarriers
dc.creator.none.fl_str_mv Rojas Delgado, Ricardo
Giacomelli, Carla Eugenia
author Rojas Delgado, Ricardo
author_facet Rojas Delgado, Ricardo
Giacomelli, Carla Eugenia
author_role author
author2 Giacomelli, Carla Eugenia
author2_role author
dc.subject.none.fl_str_mv Nanohybrids
Electrostatic Interactions
Steric Repulsion
Interfacial Modification
topic Nanohybrids
Electrostatic Interactions
Steric Repulsion
Interfacial Modification
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.10
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Layered double hydroxides (LDHs) are extensively investigated as drug nanocarriers due to their anion exchange properties and potential capacity to achieve enhanced cellular trafficking and targeted delivery. In this work, LDH–protein hybrids with controlled particle size were obtained by modulation of the charge and hydrophobicity of LDH matrixes. In order to do that, bovine serum albumin (BSA) adsorption was studied in LDH matrixes intercalated with chloride and dodecylsulfate (DS−) in different ratios and its dependence on pH and ionic strength was determined. Positively charged LDH-Cl matrixes in aqueous solution changed from micro- to nano-size when adsorbing BSA molecules at pH values higher than the isoelectric point of the protein. On the other hand, the low BSA hybridization with a negatively charged LDH-DS matrix was not enough to reduce its particle size. However, a fine tuning of the physicochemical properties of the LDH-Cl matrix by controlled DS− incorporation and pH and ionic strength conditions allowed LDH–BSA nanohybrids to be partially intercalated with the surfactant that exhibited colloidal stability at high ionic strength (similar to that of biological fluids).
Fil: Rojas Delgado, Ricardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
Fil: Giacomelli, Carla Eugenia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
description Layered double hydroxides (LDHs) are extensively investigated as drug nanocarriers due to their anion exchange properties and potential capacity to achieve enhanced cellular trafficking and targeted delivery. In this work, LDH–protein hybrids with controlled particle size were obtained by modulation of the charge and hydrophobicity of LDH matrixes. In order to do that, bovine serum albumin (BSA) adsorption was studied in LDH matrixes intercalated with chloride and dodecylsulfate (DS−) in different ratios and its dependence on pH and ionic strength was determined. Positively charged LDH-Cl matrixes in aqueous solution changed from micro- to nano-size when adsorbing BSA molecules at pH values higher than the isoelectric point of the protein. On the other hand, the low BSA hybridization with a negatively charged LDH-DS matrix was not enough to reduce its particle size. However, a fine tuning of the physicochemical properties of the LDH-Cl matrix by controlled DS− incorporation and pH and ionic strength conditions allowed LDH–BSA nanohybrids to be partially intercalated with the surfactant that exhibited colloidal stability at high ionic strength (similar to that of biological fluids).
publishDate 2015
dc.date.none.fl_str_mv 2015-02-18
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/11336/47135
Rojas Delgado, Ricardo; Giacomelli, Carla Eugenia; Size-tunable LDH-protein hybrids towards the optimization of drug nanocarriers; Royal Society of Chemistry; Journal of Materials Chemistry B; 3; 14; 18-2-2015; 2778-2785
2050-750X
2050-7518
CONICET Digital
CONICET
url http://hdl.handle.net/11336/47135
identifier_str_mv Rojas Delgado, Ricardo; Giacomelli, Carla Eugenia; Size-tunable LDH-protein hybrids towards the optimization of drug nanocarriers; Royal Society of Chemistry; Journal of Materials Chemistry B; 3; 14; 18-2-2015; 2778-2785
2050-750X
2050-7518
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2015/TB/C4TB01992J#
info:eu-repo/semantics/altIdentifier/doi/10.1039/c4tb01992j
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Royal Society of Chemistry
publisher.none.fl_str_mv Royal Society of Chemistry
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
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