Early stages of LDL oxidation: apolipoprotein B structural changes monitored by infrared spectroscopy.

Autores
Chehin, Rosana Nieves; Rengel, David; Milicua, José Carlos G.; Goñi, Félix M.; Arrondo JL; Pifat, Greta
Año de publicación
2001
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Changes in the conformation of apoliprotein B-100 in the early stages of copper-mediated low density lipoprotein oxidation have been monitored by infrared spectroscopy. During the lag phase no variation in structure is observed, indicating that copper binding to the protein does not significantly affect its structure. In the propagation phase, while hydroperoxides are formed but the protein is not modified, no changes in secondary structure are observed, but the thermal profile of the band corresponding to alpha-helix is displaced in frequency, indicating changes in tertiary structure associated with this conformation but not with beta-sheet components. When aldehyde formation starts, a decrease of approximately 3% in the area of bands corresponding to alpha-helix and beta-sheet is produced, concomitantly with an increase in beta-turns and unordered structure. The two bands corresponding to beta-turns vary as well under these conditions, indicating changes in these structures. Also at this stage the thermal profile shows variations in frequency for the bands corresponding to both alpha-helix and beta-sheet.The results are consistent with the hypothesis that as soon as the polyunsaturated fatty acids from the particle core are modified, this change is reflected at the surface, in the alpha-helical components contacting the monolayer.
Fil: Chehin, Rosana Nieves. Consejo Superior de Investigaciones Científicas; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina. Universidad del País Vasco; España
Fil: Rengel, David. Consejo Superior de Investigaciones Científicas; España. Universidad del País Vasco; España
Fil: Milicua, José Carlos G.. Universidad del País Vasco; España. Consejo Superior de Investigaciones Científicas; España
Fil: Goñi, Félix M.. Universidad del País Vasco; España. Consejo Superior de Investigaciones Científicas; España
Fil: Arrondo JL. Consejo Superior de Investigaciones Científicas; España. Universidad del País Vasco; España
Fil: Pifat, Greta. Rudjer Bošković Institute; Croacia
Materia
apoB
secondary structure
thermal denaturation
copper-mediated oxidation
atherosclerosis
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:11336/97982
Acceder
id CONICETDig_078ae60689dc7e166f5ab0a4ced3c2f2
oai_identifier_str oai:ri.conicet.gov.ar:11336/97982
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Early stages of LDL oxidation: apolipoprotein B structural changes monitored by infrared spectroscopy.Chehin, Rosana NievesRengel, DavidMilicua, José Carlos G.Goñi, Félix M.Arrondo JLPifat, GretaapoBsecondary structurethermal denaturationcopper-mediated oxidationatherosclerosishttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Changes in the conformation of apoliprotein B-100 in the early stages of copper-mediated low density lipoprotein oxidation have been monitored by infrared spectroscopy. During the lag phase no variation in structure is observed, indicating that copper binding to the protein does not significantly affect its structure. In the propagation phase, while hydroperoxides are formed but the protein is not modified, no changes in secondary structure are observed, but the thermal profile of the band corresponding to alpha-helix is displaced in frequency, indicating changes in tertiary structure associated with this conformation but not with beta-sheet components. When aldehyde formation starts, a decrease of approximately 3% in the area of bands corresponding to alpha-helix and beta-sheet is produced, concomitantly with an increase in beta-turns and unordered structure. The two bands corresponding to beta-turns vary as well under these conditions, indicating changes in these structures. Also at this stage the thermal profile shows variations in frequency for the bands corresponding to both alpha-helix and beta-sheet.The results are consistent with the hypothesis that as soon as the polyunsaturated fatty acids from the particle core are modified, this change is reflected at the surface, in the alpha-helical components contacting the monolayer.Fil: Chehin, Rosana Nieves. Consejo Superior de Investigaciones Científicas; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina. Universidad del País Vasco; EspañaFil: Rengel, David. Consejo Superior de Investigaciones Científicas; España. Universidad del País Vasco; EspañaFil: Milicua, José Carlos G.. Universidad del País Vasco; España. Consejo Superior de Investigaciones Científicas; EspañaFil: Goñi, Félix M.. Universidad del País Vasco; España. Consejo Superior de Investigaciones Científicas; EspañaFil: Arrondo JL. Consejo Superior de Investigaciones Científicas; España. Universidad del País Vasco; EspañaFil: Pifat, Greta. Rudjer Bošković Institute; CroaciaAmerican Society for Biochemistry and Molecular Biology2001-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/97982Chehin, Rosana Nieves; Rengel, David; Milicua, José Carlos G.; Goñi, Félix M.; Arrondo JL; et al.; Early stages of LDL oxidation: apolipoprotein B structural changes monitored by infrared spectroscopy.; American Society for Biochemistry and Molecular Biology; Journal of Lipid Research Papers In Press; 42; 5; 12-2001; 778-7820022-22751539-7262CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.jlr.org/content/42/5/778.longinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:58:00Zoai:ri.conicet.gov.ar:11336/97982instacron: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 09:58:01.165CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Early stages of LDL oxidation: apolipoprotein B structural changes monitored by infrared spectroscopy.
title Early stages of LDL oxidation: apolipoprotein B structural changes monitored by infrared spectroscopy.
spellingShingle Early stages of LDL oxidation: apolipoprotein B structural changes monitored by infrared spectroscopy.
Chehin, Rosana Nieves
apoB
secondary structure
thermal denaturation
copper-mediated oxidation
atherosclerosis
title_short Early stages of LDL oxidation: apolipoprotein B structural changes monitored by infrared spectroscopy.
title_full Early stages of LDL oxidation: apolipoprotein B structural changes monitored by infrared spectroscopy.
title_fullStr Early stages of LDL oxidation: apolipoprotein B structural changes monitored by infrared spectroscopy.
title_full_unstemmed Early stages of LDL oxidation: apolipoprotein B structural changes monitored by infrared spectroscopy.
title_sort Early stages of LDL oxidation: apolipoprotein B structural changes monitored by infrared spectroscopy.
dc.creator.none.fl_str_mv Chehin, Rosana Nieves
Rengel, David
Milicua, José Carlos G.
Goñi, Félix M.
Arrondo JL
Pifat, Greta
author Chehin, Rosana Nieves
author_facet Chehin, Rosana Nieves
Rengel, David
Milicua, José Carlos G.
Goñi, Félix M.
Arrondo JL
Pifat, Greta
author_role author
author2 Rengel, David
Milicua, José Carlos G.
Goñi, Félix M.
Arrondo JL
Pifat, Greta
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv apoB
secondary structure
thermal denaturation
copper-mediated oxidation
atherosclerosis
topic apoB
secondary structure
thermal denaturation
copper-mediated oxidation
atherosclerosis
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Changes in the conformation of apoliprotein B-100 in the early stages of copper-mediated low density lipoprotein oxidation have been monitored by infrared spectroscopy. During the lag phase no variation in structure is observed, indicating that copper binding to the protein does not significantly affect its structure. In the propagation phase, while hydroperoxides are formed but the protein is not modified, no changes in secondary structure are observed, but the thermal profile of the band corresponding to alpha-helix is displaced in frequency, indicating changes in tertiary structure associated with this conformation but not with beta-sheet components. When aldehyde formation starts, a decrease of approximately 3% in the area of bands corresponding to alpha-helix and beta-sheet is produced, concomitantly with an increase in beta-turns and unordered structure. The two bands corresponding to beta-turns vary as well under these conditions, indicating changes in these structures. Also at this stage the thermal profile shows variations in frequency for the bands corresponding to both alpha-helix and beta-sheet.The results are consistent with the hypothesis that as soon as the polyunsaturated fatty acids from the particle core are modified, this change is reflected at the surface, in the alpha-helical components contacting the monolayer.
Fil: Chehin, Rosana Nieves. Consejo Superior de Investigaciones Científicas; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina. Universidad del País Vasco; España
Fil: Rengel, David. Consejo Superior de Investigaciones Científicas; España. Universidad del País Vasco; España
Fil: Milicua, José Carlos G.. Universidad del País Vasco; España. Consejo Superior de Investigaciones Científicas; España
Fil: Goñi, Félix M.. Universidad del País Vasco; España. Consejo Superior de Investigaciones Científicas; España
Fil: Arrondo JL. Consejo Superior de Investigaciones Científicas; España. Universidad del País Vasco; España
Fil: Pifat, Greta. Rudjer Bošković Institute; Croacia
description Changes in the conformation of apoliprotein B-100 in the early stages of copper-mediated low density lipoprotein oxidation have been monitored by infrared spectroscopy. During the lag phase no variation in structure is observed, indicating that copper binding to the protein does not significantly affect its structure. In the propagation phase, while hydroperoxides are formed but the protein is not modified, no changes in secondary structure are observed, but the thermal profile of the band corresponding to alpha-helix is displaced in frequency, indicating changes in tertiary structure associated with this conformation but not with beta-sheet components. When aldehyde formation starts, a decrease of approximately 3% in the area of bands corresponding to alpha-helix and beta-sheet is produced, concomitantly with an increase in beta-turns and unordered structure. The two bands corresponding to beta-turns vary as well under these conditions, indicating changes in these structures. Also at this stage the thermal profile shows variations in frequency for the bands corresponding to both alpha-helix and beta-sheet.The results are consistent with the hypothesis that as soon as the polyunsaturated fatty acids from the particle core are modified, this change is reflected at the surface, in the alpha-helical components contacting the monolayer.
publishDate 2001
dc.date.none.fl_str_mv 2001-12
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/11336/97982
Chehin, Rosana Nieves; Rengel, David; Milicua, José Carlos G.; Goñi, Félix M.; Arrondo JL; et al.; Early stages of LDL oxidation: apolipoprotein B structural changes monitored by infrared spectroscopy.; American Society for Biochemistry and Molecular Biology; Journal of Lipid Research Papers In Press; 42; 5; 12-2001; 778-782
0022-2275
1539-7262
CONICET Digital
CONICET
url http://hdl.handle.net/11336/97982
identifier_str_mv Chehin, Rosana Nieves; Rengel, David; Milicua, José Carlos G.; Goñi, Félix M.; Arrondo JL; et al.; Early stages of LDL oxidation: apolipoprotein B structural changes monitored by infrared spectroscopy.; American Society for Biochemistry and Molecular Biology; Journal of Lipid Research Papers In Press; 42; 5; 12-2001; 778-782
0022-2275
1539-7262
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://www.jlr.org/content/42/5/778.long
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
dc.publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
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_ 1842269495570202624
score 13.13397

Publicaciones similares