Interactions between DMPC Liposomes and the Serum Blood Proteins HSA and IgG
- Autores
- Sabín Fernández, Juan Daniel; Prieto, Gerardo; Ruso, Juan M.; Messina, Paula Verónica; Salgado, Francisco J.; Nogueira, Montserrat; Costas, Miguel; Sarmiento, Felix
- Año de publicación
- 2009
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The interaction between two serum blood proteins, namely human serum albumin (HSA) and human immunoglobulin G (IgG), with 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) liposomes has been studied in detail using dynamic light scattering, flow cytometry, enzyme-linked immunosorbent assay (ELISA), electrophoretic mobility, differential scanning calorimetry (DSC), and surface tension measurements. HSA and IgG interact with liposomes forming molecular aggregates that remain stable at protein concentrations beyond those of total liposome coverage. Both HSA and IgG penetrate into the liposome bilayer. An ELISA assay indicates that the Fc region of IgG is the one that is immersed in the DMPC membrane. The liposome−protein interaction is mainly of electrostatic nature, but an important hydrophobic contribution is also present.
Fil: Sabín Fernández, Juan Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Santiago de Compostela. Facultad de Física; España
Fil: Prieto, Gerardo. Universidad de Santiago de Compostela. Facultad de Física; España
Fil: Ruso, Juan M.. Universidad de Santiago de Compostela. Facultad de Física; España
Fil: Messina, Paula Verónica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina
Fil: Salgado, Francisco J.. Universidad de Santiago de Compostela; España
Fil: Nogueira, Montserrat. Universidad de Santiago de Compostela. Facultad de Química; España
Fil: Costas, Miguel. Universidad Nacional Autonoma de Mexico. Facultad de Ciencias; México
Fil: Sarmiento, Felix. Universidad de Santiago de Compostela. Facultad de Física; España - Materia
-
Liposomes
Igg
Hsa
Proteins - 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:11336/66177
Ver los metadatos del registro completo
id |
CONICETDig_2900de4a0d17b717cfb2fd68f75c5313 |
---|---|
oai_identifier_str |
oai:ri.conicet.gov.ar:11336/66177 |
network_acronym_str |
CONICETDig |
repository_id_str |
3498 |
network_name_str |
CONICET Digital (CONICET) |
spelling |
Interactions between DMPC Liposomes and the Serum Blood Proteins HSA and IgGSabín Fernández, Juan DanielPrieto, GerardoRuso, Juan M.Messina, Paula VerónicaSalgado, Francisco J.Nogueira, MontserratCostas, MiguelSarmiento, FelixLiposomesIggHsaProteinshttps://purl.org/becyt/ford/1.3https://purl.org/becyt/ford/1The interaction between two serum blood proteins, namely human serum albumin (HSA) and human immunoglobulin G (IgG), with 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) liposomes has been studied in detail using dynamic light scattering, flow cytometry, enzyme-linked immunosorbent assay (ELISA), electrophoretic mobility, differential scanning calorimetry (DSC), and surface tension measurements. HSA and IgG interact with liposomes forming molecular aggregates that remain stable at protein concentrations beyond those of total liposome coverage. Both HSA and IgG penetrate into the liposome bilayer. An ELISA assay indicates that the Fc region of IgG is the one that is immersed in the DMPC membrane. The liposome−protein interaction is mainly of electrostatic nature, but an important hydrophobic contribution is also present.Fil: Sabín Fernández, Juan Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Santiago de Compostela. Facultad de Física; EspañaFil: Prieto, Gerardo. Universidad de Santiago de Compostela. Facultad de Física; EspañaFil: Ruso, Juan M.. Universidad de Santiago de Compostela. Facultad de Física; EspañaFil: Messina, Paula Verónica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; ArgentinaFil: Salgado, Francisco J.. Universidad de Santiago de Compostela; EspañaFil: Nogueira, Montserrat. Universidad de Santiago de Compostela. Facultad de Química; EspañaFil: Costas, Miguel. Universidad Nacional Autonoma de Mexico. Facultad de Ciencias; MéxicoFil: Sarmiento, Felix. Universidad de Santiago de Compostela. Facultad de Física; EspañaAmerican Chemical Society2009-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/66177Sabín Fernández, Juan Daniel; Prieto, Gerardo; Ruso, Juan M.; Messina, Paula Verónica; Salgado, Francisco J.; et al.; Interactions between DMPC Liposomes and the Serum Blood Proteins HSA and IgG; American Chemical Society; Journal of Physical Chemistry B; 113; 6; 2-2009; 1655-16611520-6106CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/abs/10.1021/jp804641einfo:eu-repo/semantics/altIdentifier/doi/10.1021/jp804641einfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:55:43Zoai:ri.conicet.gov.ar:11336/66177instacron: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:34982025-09-03 09:55:43.726CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Interactions between DMPC Liposomes and the Serum Blood Proteins HSA and IgG |
title |
Interactions between DMPC Liposomes and the Serum Blood Proteins HSA and IgG |
spellingShingle |
Interactions between DMPC Liposomes and the Serum Blood Proteins HSA and IgG Sabín Fernández, Juan Daniel Liposomes Igg Hsa Proteins |
title_short |
Interactions between DMPC Liposomes and the Serum Blood Proteins HSA and IgG |
title_full |
Interactions between DMPC Liposomes and the Serum Blood Proteins HSA and IgG |
title_fullStr |
Interactions between DMPC Liposomes and the Serum Blood Proteins HSA and IgG |
title_full_unstemmed |
Interactions between DMPC Liposomes and the Serum Blood Proteins HSA and IgG |
title_sort |
Interactions between DMPC Liposomes and the Serum Blood Proteins HSA and IgG |
dc.creator.none.fl_str_mv |
Sabín Fernández, Juan Daniel Prieto, Gerardo Ruso, Juan M. Messina, Paula Verónica Salgado, Francisco J. Nogueira, Montserrat Costas, Miguel Sarmiento, Felix |
author |
Sabín Fernández, Juan Daniel |
author_facet |
Sabín Fernández, Juan Daniel Prieto, Gerardo Ruso, Juan M. Messina, Paula Verónica Salgado, Francisco J. Nogueira, Montserrat Costas, Miguel Sarmiento, Felix |
author_role |
author |
author2 |
Prieto, Gerardo Ruso, Juan M. Messina, Paula Verónica Salgado, Francisco J. Nogueira, Montserrat Costas, Miguel Sarmiento, Felix |
author2_role |
author author author author author author author |
dc.subject.none.fl_str_mv |
Liposomes Igg Hsa Proteins |
topic |
Liposomes Igg Hsa Proteins |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.3 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
The interaction between two serum blood proteins, namely human serum albumin (HSA) and human immunoglobulin G (IgG), with 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) liposomes has been studied in detail using dynamic light scattering, flow cytometry, enzyme-linked immunosorbent assay (ELISA), electrophoretic mobility, differential scanning calorimetry (DSC), and surface tension measurements. HSA and IgG interact with liposomes forming molecular aggregates that remain stable at protein concentrations beyond those of total liposome coverage. Both HSA and IgG penetrate into the liposome bilayer. An ELISA assay indicates that the Fc region of IgG is the one that is immersed in the DMPC membrane. The liposome−protein interaction is mainly of electrostatic nature, but an important hydrophobic contribution is also present. Fil: Sabín Fernández, Juan Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Santiago de Compostela. Facultad de Física; España Fil: Prieto, Gerardo. Universidad de Santiago de Compostela. Facultad de Física; España Fil: Ruso, Juan M.. Universidad de Santiago de Compostela. Facultad de Física; España Fil: Messina, Paula Verónica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Química del Sur. Universidad Nacional del Sur. Departamento de Química. Instituto de Química del Sur; Argentina Fil: Salgado, Francisco J.. Universidad de Santiago de Compostela; España Fil: Nogueira, Montserrat. Universidad de Santiago de Compostela. Facultad de Química; España Fil: Costas, Miguel. Universidad Nacional Autonoma de Mexico. Facultad de Ciencias; México Fil: Sarmiento, Felix. Universidad de Santiago de Compostela. Facultad de Física; España |
description |
The interaction between two serum blood proteins, namely human serum albumin (HSA) and human immunoglobulin G (IgG), with 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) liposomes has been studied in detail using dynamic light scattering, flow cytometry, enzyme-linked immunosorbent assay (ELISA), electrophoretic mobility, differential scanning calorimetry (DSC), and surface tension measurements. HSA and IgG interact with liposomes forming molecular aggregates that remain stable at protein concentrations beyond those of total liposome coverage. Both HSA and IgG penetrate into the liposome bilayer. An ELISA assay indicates that the Fc region of IgG is the one that is immersed in the DMPC membrane. The liposome−protein interaction is mainly of electrostatic nature, but an important hydrophobic contribution is also present. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-02 |
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/11336/66177 Sabín Fernández, Juan Daniel; Prieto, Gerardo; Ruso, Juan M.; Messina, Paula Verónica; Salgado, Francisco J.; et al.; Interactions between DMPC Liposomes and the Serum Blood Proteins HSA and IgG; American Chemical Society; Journal of Physical Chemistry B; 113; 6; 2-2009; 1655-1661 1520-6106 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/66177 |
identifier_str_mv |
Sabín Fernández, Juan Daniel; Prieto, Gerardo; Ruso, Juan M.; Messina, Paula Verónica; Salgado, Francisco J.; et al.; Interactions between DMPC Liposomes and the Serum Blood Proteins HSA and IgG; American Chemical Society; Journal of Physical Chemistry B; 113; 6; 2-2009; 1655-1661 1520-6106 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://pubs.acs.org/doi/abs/10.1021/jp804641e info:eu-repo/semantics/altIdentifier/doi/10.1021/jp804641e |
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 |
dc.publisher.none.fl_str_mv |
American Chemical Society |
publisher.none.fl_str_mv |
American Chemical Society |
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_ |
1842269362520588288 |
score |
13.13397 |