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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/47135
Ver los metadatos del registro completo
id |
CONICETDig_e2125d7261b93b76d6192b5ce800a0f9 |
---|---|
oai_identifier_str |
oai:ri.conicet.gov.ar:11336/47135 |
network_acronym_str |
CONICETDig |
repository_id_str |
3498 |
network_name_str |
CONICET Digital (CONICET) |
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 |
_version_ |
1844614423201710080 |
score |
13.070432 |