Surface characterization of human serum albumin and sodium perfluorooctanoate mixed solutions by pendant drop tensiometry and circular dichroism

Autores
Messina, Paula Verónica; Prieto, Gerardo; Dodero, Veronica Isabel; Cabrerizo-Vilchez, M.A.; Maldonado Valderrama, J.; Ruso, Juan M.; Sarmiento, Félix
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The interfacial behavior of mixed human serum albumin (HSA)/sodium perfluorooctanoate (C8FONa) solutions is examined by using two experimental techniques, pendant drop tensiometry and circular dichroism spectroscopy. Through the analysis of the surface tension of the mixed solutions, surface competitive adsorption at the air-water interface between C8FONa and HSA is detected. The dynamic adsorption curves exhibit the distinct regimes in their time-dependent surface tension. The nature of these regimes is further analyzed in terms of the variation of the molecules surface areas. As a consequence, a compact and dense structure was formed where protein molecules were interconnected and overlapped. Thus, a reduction of the area occupied per molecule from 100 to 0.2 nm2 is interpreted as a gel-like structure at the surface. The presence of the surfactant seems to favor the formation of this interfacial structure. Finally, measurements of circular dichroism suggests a compaction of the protein due to the association with the surfactant given by an increase of α-helix structure in the complexes as compared to that of pure protein.
Fil: Messina, Paula Verónica. Universidad de Santiago de Compostela; España. 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: Prieto, Gerardo. Universidad de Santiago de Compostela; España
Fil: Dodero, Veronica Isabel. Universidad de Santiago de Compostela; España. 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: Cabrerizo-Vilchez, M.A.. Universidad de Granada. Facultad de Ciencias; España
Fil: Maldonado Valderrama, J.. Universidad de Granada. Facultad de Ciencias; España
Fil: Ruso, Juan M.. Universidad de Santiago de Compostela; España
Fil: Sarmiento, Félix. Universidad de Santiago de Compostela; España
Materia
CIRCULAR DICHROISM
HUMAN SERUM ALBUMIN
PENDANT DROP TENSIOMETRY
SODIUM PERFLUOROOCTANOATE
SURFACE CHARACTERIZATION
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:11336/95355
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/95355
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Surface characterization of human serum albumin and sodium perfluorooctanoate mixed solutions by pendant drop tensiometry and circular dichroismMessina, Paula VerónicaPrieto, GerardoDodero, Veronica IsabelCabrerizo-Vilchez, M.A.Maldonado Valderrama, J.Ruso, Juan M.Sarmiento, FélixCIRCULAR DICHROISMHUMAN SERUM ALBUMINPENDANT DROP TENSIOMETRYSODIUM PERFLUOROOCTANOATESURFACE CHARACTERIZATIONhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The interfacial behavior of mixed human serum albumin (HSA)/sodium perfluorooctanoate (C8FONa) solutions is examined by using two experimental techniques, pendant drop tensiometry and circular dichroism spectroscopy. Through the analysis of the surface tension of the mixed solutions, surface competitive adsorption at the air-water interface between C8FONa and HSA is detected. The dynamic adsorption curves exhibit the distinct regimes in their time-dependent surface tension. The nature of these regimes is further analyzed in terms of the variation of the molecules surface areas. As a consequence, a compact and dense structure was formed where protein molecules were interconnected and overlapped. Thus, a reduction of the area occupied per molecule from 100 to 0.2 nm2 is interpreted as a gel-like structure at the surface. The presence of the surfactant seems to favor the formation of this interfacial structure. Finally, measurements of circular dichroism suggests a compaction of the protein due to the association with the surfactant given by an increase of α-helix structure in the complexes as compared to that of pure protein.Fil: Messina, Paula Verónica. Universidad de Santiago de Compostela; España. 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: Prieto, Gerardo. Universidad de Santiago de Compostela; EspañaFil: Dodero, Veronica Isabel. Universidad de Santiago de Compostela; España. 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: Cabrerizo-Vilchez, M.A.. Universidad de Granada. Facultad de Ciencias; EspañaFil: Maldonado Valderrama, J.. Universidad de Granada. Facultad de Ciencias; EspañaFil: Ruso, Juan M.. Universidad de Santiago de Compostela; EspañaFil: Sarmiento, Félix. Universidad de Santiago de Compostela; EspañaJohn Wiley & Sons Inc2006-06info: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/11336/95355Messina, Paula Verónica; Prieto, Gerardo; Dodero, Veronica Isabel; Cabrerizo-Vilchez, M.A.; Maldonado Valderrama, J.; et al.; Surface characterization of human serum albumin and sodium perfluorooctanoate mixed solutions by pendant drop tensiometry and circular dichroism; John Wiley & Sons Inc; Biopolymers; 82; 3; 6-2006; 261-2710006-3525CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1002/bip.20494info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/bip.20494info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:47:54Zoai:ri.conicet.gov.ar:11336/95355instacron: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 10:47:54.526CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Surface characterization of human serum albumin and sodium perfluorooctanoate mixed solutions by pendant drop tensiometry and circular dichroism
title Surface characterization of human serum albumin and sodium perfluorooctanoate mixed solutions by pendant drop tensiometry and circular dichroism
spellingShingle Surface characterization of human serum albumin and sodium perfluorooctanoate mixed solutions by pendant drop tensiometry and circular dichroism
Messina, Paula Verónica
CIRCULAR DICHROISM
HUMAN SERUM ALBUMIN
PENDANT DROP TENSIOMETRY
SODIUM PERFLUOROOCTANOATE
SURFACE CHARACTERIZATION
title_short Surface characterization of human serum albumin and sodium perfluorooctanoate mixed solutions by pendant drop tensiometry and circular dichroism
title_full Surface characterization of human serum albumin and sodium perfluorooctanoate mixed solutions by pendant drop tensiometry and circular dichroism
title_fullStr Surface characterization of human serum albumin and sodium perfluorooctanoate mixed solutions by pendant drop tensiometry and circular dichroism
title_full_unstemmed Surface characterization of human serum albumin and sodium perfluorooctanoate mixed solutions by pendant drop tensiometry and circular dichroism
title_sort Surface characterization of human serum albumin and sodium perfluorooctanoate mixed solutions by pendant drop tensiometry and circular dichroism
dc.creator.none.fl_str_mv Messina, Paula Verónica
Prieto, Gerardo
Dodero, Veronica Isabel
Cabrerizo-Vilchez, M.A.
Maldonado Valderrama, J.
Ruso, Juan M.
Sarmiento, Félix
author Messina, Paula Verónica
author_facet Messina, Paula Verónica
Prieto, Gerardo
Dodero, Veronica Isabel
Cabrerizo-Vilchez, M.A.
Maldonado Valderrama, J.
Ruso, Juan M.
Sarmiento, Félix
author_role author
author2 Prieto, Gerardo
Dodero, Veronica Isabel
Cabrerizo-Vilchez, M.A.
Maldonado Valderrama, J.
Ruso, Juan M.
Sarmiento, Félix
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv CIRCULAR DICHROISM
HUMAN SERUM ALBUMIN
PENDANT DROP TENSIOMETRY
SODIUM PERFLUOROOCTANOATE
SURFACE CHARACTERIZATION
topic CIRCULAR DICHROISM
HUMAN SERUM ALBUMIN
PENDANT DROP TENSIOMETRY
SODIUM PERFLUOROOCTANOATE
SURFACE CHARACTERIZATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The interfacial behavior of mixed human serum albumin (HSA)/sodium perfluorooctanoate (C8FONa) solutions is examined by using two experimental techniques, pendant drop tensiometry and circular dichroism spectroscopy. Through the analysis of the surface tension of the mixed solutions, surface competitive adsorption at the air-water interface between C8FONa and HSA is detected. The dynamic adsorption curves exhibit the distinct regimes in their time-dependent surface tension. The nature of these regimes is further analyzed in terms of the variation of the molecules surface areas. As a consequence, a compact and dense structure was formed where protein molecules were interconnected and overlapped. Thus, a reduction of the area occupied per molecule from 100 to 0.2 nm2 is interpreted as a gel-like structure at the surface. The presence of the surfactant seems to favor the formation of this interfacial structure. Finally, measurements of circular dichroism suggests a compaction of the protein due to the association with the surfactant given by an increase of α-helix structure in the complexes as compared to that of pure protein.
Fil: Messina, Paula Verónica. Universidad de Santiago de Compostela; España. 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: Prieto, Gerardo. Universidad de Santiago de Compostela; España
Fil: Dodero, Veronica Isabel. Universidad de Santiago de Compostela; España. 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: Cabrerizo-Vilchez, M.A.. Universidad de Granada. Facultad de Ciencias; España
Fil: Maldonado Valderrama, J.. Universidad de Granada. Facultad de Ciencias; España
Fil: Ruso, Juan M.. Universidad de Santiago de Compostela; España
Fil: Sarmiento, Félix. Universidad de Santiago de Compostela; España
description The interfacial behavior of mixed human serum albumin (HSA)/sodium perfluorooctanoate (C8FONa) solutions is examined by using two experimental techniques, pendant drop tensiometry and circular dichroism spectroscopy. Through the analysis of the surface tension of the mixed solutions, surface competitive adsorption at the air-water interface between C8FONa and HSA is detected. The dynamic adsorption curves exhibit the distinct regimes in their time-dependent surface tension. The nature of these regimes is further analyzed in terms of the variation of the molecules surface areas. As a consequence, a compact and dense structure was formed where protein molecules were interconnected and overlapped. Thus, a reduction of the area occupied per molecule from 100 to 0.2 nm2 is interpreted as a gel-like structure at the surface. The presence of the surfactant seems to favor the formation of this interfacial structure. Finally, measurements of circular dichroism suggests a compaction of the protein due to the association with the surfactant given by an increase of α-helix structure in the complexes as compared to that of pure protein.
publishDate 2006
dc.date.none.fl_str_mv 2006-06
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/11336/95355
Messina, Paula Verónica; Prieto, Gerardo; Dodero, Veronica Isabel; Cabrerizo-Vilchez, M.A.; Maldonado Valderrama, J.; et al.; Surface characterization of human serum albumin and sodium perfluorooctanoate mixed solutions by pendant drop tensiometry and circular dichroism; John Wiley & Sons Inc; Biopolymers; 82; 3; 6-2006; 261-271
0006-3525
CONICET Digital
CONICET
url http://hdl.handle.net/11336/95355
identifier_str_mv Messina, Paula Verónica; Prieto, Gerardo; Dodero, Veronica Isabel; Cabrerizo-Vilchez, M.A.; Maldonado Valderrama, J.; et al.; Surface characterization of human serum albumin and sodium perfluorooctanoate mixed solutions by pendant drop tensiometry and circular dichroism; John Wiley & Sons Inc; Biopolymers; 82; 3; 6-2006; 261-271
0006-3525
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1002/bip.20494
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1002/bip.20494
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 John Wiley & Sons Inc
publisher.none.fl_str_mv John Wiley & Sons Inc
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_ 1844614524085207040
score 13.070432

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