The lipid-mediated hypothesis of fumonisin B1 toxicodynamics tested in model membranes

Autores
Theumer, Martín Gustavo; Clop, Eduardo Matias; Rubinstein, Héctor Ramón; Perillo, Maria Angelica
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The disruption of lipidic metabolism was considered a good candidate to explain FB1 toxicity mechanism. In the present work we investigated molecular organizational changes induced by FB1-biomembrane interaction possibly involved in mycotoxic effects. FB1 was self-aggregated with a critical micellar concentration of 1.97 mM. FB1 (0-81.4 μM), decreased in a dose-dependent manner, the fluorescence anisotropy of TMA-DPH (from 0.349 ± 0.003 to 0.1720 ± 0.0035) in dpPC bilayers, whilst no differences were registered with DPH. At 5.6 μM in the subphase, FB1 increased the lateral surface pressure (π) of a Langmuir film to an extent that depended on the monolayer composition (ΔπdpPC:DOTAP 3:1 > ΔπdpPC:dpPA3:1 > ΔπdpPC), the molecular packing (Δπ decreased linearly as a function of the initial π) and the subphase pH (ΔπpH 2.6 > ΔπpH 7.4 and maximal π allowing the drug penetration πcut-off was 34.3 and 27.7 mN/m at pH 2.63 and 7.4, respectively). FB1 increased the surface potential of dpPC and dpPC:DOTAP monolayers and decreased that of dpPC:dpPA. This suggested that FB1 acquired different orientations and/or foldings depending on the surface electrostatics and the toxin charge state. Moreover, FB1-lipid interactions were transduced into long-range effects at the mesoscopic level affecting the lipidic self-separated lateral domains shape and density.
Fil: Theumer, Martín Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba; Argentina
Fil: Clop, Eduardo Matias. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina. Universidad Nacional de Cordoba. Facultad de Ciencias Exactas Fisicas y Naturales. Departamento de Quimica; Argentina
Fil: Rubinstein, Héctor Ramón. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Bioquímica Clínica; Argentina. Universidad Nacional de Córdoba. Secretaría de Ciencia y Tecnología. Instituto Superior de Investigación, Desarrollo y Servicio de Alimentos; Argentina
Fil: Perillo, Maria Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina. Universidad Nacional de Cordoba. Facultad de Ciencias Exactas Fisicas y Naturales. Departamento de Quimica; Argentina
Materia
Folding
Fumonisin B1
Membrane-Binding Interfacial Localization
Mycotoxins
Self-Aggregation
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:11336/57747
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/57747
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The lipid-mediated hypothesis of fumonisin B1 toxicodynamics tested in model membranesTheumer, Martín GustavoClop, Eduardo MatiasRubinstein, Héctor RamónPerillo, Maria AngelicaFoldingFumonisin B1Membrane-Binding Interfacial LocalizationMycotoxinsSelf-Aggregationhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The disruption of lipidic metabolism was considered a good candidate to explain FB1 toxicity mechanism. In the present work we investigated molecular organizational changes induced by FB1-biomembrane interaction possibly involved in mycotoxic effects. FB1 was self-aggregated with a critical micellar concentration of 1.97 mM. FB1 (0-81.4 μM), decreased in a dose-dependent manner, the fluorescence anisotropy of TMA-DPH (from 0.349 ± 0.003 to 0.1720 ± 0.0035) in dpPC bilayers, whilst no differences were registered with DPH. At 5.6 μM in the subphase, FB1 increased the lateral surface pressure (π) of a Langmuir film to an extent that depended on the monolayer composition (ΔπdpPC:DOTAP 3:1 > ΔπdpPC:dpPA3:1 > ΔπdpPC), the molecular packing (Δπ decreased linearly as a function of the initial π) and the subphase pH (ΔπpH 2.6 > ΔπpH 7.4 and maximal π allowing the drug penetration πcut-off was 34.3 and 27.7 mN/m at pH 2.63 and 7.4, respectively). FB1 increased the surface potential of dpPC and dpPC:DOTAP monolayers and decreased that of dpPC:dpPA. This suggested that FB1 acquired different orientations and/or foldings depending on the surface electrostatics and the toxin charge state. Moreover, FB1-lipid interactions were transduced into long-range effects at the mesoscopic level affecting the lipidic self-separated lateral domains shape and density.Fil: Theumer, Martín Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba; ArgentinaFil: Clop, Eduardo Matias. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina. Universidad Nacional de Cordoba. Facultad de Ciencias Exactas Fisicas y Naturales. Departamento de Quimica; ArgentinaFil: Rubinstein, Héctor Ramón. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Bioquímica Clínica; Argentina. Universidad Nacional de Córdoba. Secretaría de Ciencia y Tecnología. Instituto Superior de Investigación, Desarrollo y Servicio de Alimentos; ArgentinaFil: Perillo, Maria Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina. Universidad Nacional de Cordoba. Facultad de Ciencias Exactas Fisicas y Naturales. Departamento de Quimica; ArgentinaElsevier Science2008-06-15info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/57747Theumer, Martín Gustavo; Clop, Eduardo Matias; Rubinstein, Héctor Ramón; Perillo, Maria Angelica; The lipid-mediated hypothesis of fumonisin B1 toxicodynamics tested in model membranes; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 64; 1; 15-6-2008; 22-330927-7765CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0927776508000052info:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfb.2008.01.002info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:36:00Zoai:ri.conicet.gov.ar:11336/57747instacron: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:34982025-10-22 11:36:00.658CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The lipid-mediated hypothesis of fumonisin B1 toxicodynamics tested in model membranes
title The lipid-mediated hypothesis of fumonisin B1 toxicodynamics tested in model membranes
spellingShingle The lipid-mediated hypothesis of fumonisin B1 toxicodynamics tested in model membranes
Theumer, Martín Gustavo
Folding
Fumonisin B1
Membrane-Binding Interfacial Localization
Mycotoxins
Self-Aggregation
title_short The lipid-mediated hypothesis of fumonisin B1 toxicodynamics tested in model membranes
title_full The lipid-mediated hypothesis of fumonisin B1 toxicodynamics tested in model membranes
title_fullStr The lipid-mediated hypothesis of fumonisin B1 toxicodynamics tested in model membranes
title_full_unstemmed The lipid-mediated hypothesis of fumonisin B1 toxicodynamics tested in model membranes
title_sort The lipid-mediated hypothesis of fumonisin B1 toxicodynamics tested in model membranes
dc.creator.none.fl_str_mv Theumer, Martín Gustavo
Clop, Eduardo Matias
Rubinstein, Héctor Ramón
Perillo, Maria Angelica
author Theumer, Martín Gustavo
author_facet Theumer, Martín Gustavo
Clop, Eduardo Matias
Rubinstein, Héctor Ramón
Perillo, Maria Angelica
author_role author
author2 Clop, Eduardo Matias
Rubinstein, Héctor Ramón
Perillo, Maria Angelica
author2_role author
author
author
dc.subject.none.fl_str_mv Folding
Fumonisin B1
Membrane-Binding Interfacial Localization
Mycotoxins
Self-Aggregation
topic Folding
Fumonisin B1
Membrane-Binding Interfacial Localization
Mycotoxins
Self-Aggregation
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The disruption of lipidic metabolism was considered a good candidate to explain FB1 toxicity mechanism. In the present work we investigated molecular organizational changes induced by FB1-biomembrane interaction possibly involved in mycotoxic effects. FB1 was self-aggregated with a critical micellar concentration of 1.97 mM. FB1 (0-81.4 μM), decreased in a dose-dependent manner, the fluorescence anisotropy of TMA-DPH (from 0.349 ± 0.003 to 0.1720 ± 0.0035) in dpPC bilayers, whilst no differences were registered with DPH. At 5.6 μM in the subphase, FB1 increased the lateral surface pressure (π) of a Langmuir film to an extent that depended on the monolayer composition (ΔπdpPC:DOTAP 3:1 > ΔπdpPC:dpPA3:1 > ΔπdpPC), the molecular packing (Δπ decreased linearly as a function of the initial π) and the subphase pH (ΔπpH 2.6 > ΔπpH 7.4 and maximal π allowing the drug penetration πcut-off was 34.3 and 27.7 mN/m at pH 2.63 and 7.4, respectively). FB1 increased the surface potential of dpPC and dpPC:DOTAP monolayers and decreased that of dpPC:dpPA. This suggested that FB1 acquired different orientations and/or foldings depending on the surface electrostatics and the toxin charge state. Moreover, FB1-lipid interactions were transduced into long-range effects at the mesoscopic level affecting the lipidic self-separated lateral domains shape and density.
Fil: Theumer, Martín Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba; Argentina
Fil: Clop, Eduardo Matias. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina. Universidad Nacional de Cordoba. Facultad de Ciencias Exactas Fisicas y Naturales. Departamento de Quimica; Argentina
Fil: Rubinstein, Héctor Ramón. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Bioquímica Clínica; Argentina. Universidad Nacional de Córdoba. Secretaría de Ciencia y Tecnología. Instituto Superior de Investigación, Desarrollo y Servicio de Alimentos; Argentina
Fil: Perillo, Maria Angelica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina. Universidad Nacional de Cordoba. Facultad de Ciencias Exactas Fisicas y Naturales. Departamento de Quimica; Argentina
description The disruption of lipidic metabolism was considered a good candidate to explain FB1 toxicity mechanism. In the present work we investigated molecular organizational changes induced by FB1-biomembrane interaction possibly involved in mycotoxic effects. FB1 was self-aggregated with a critical micellar concentration of 1.97 mM. FB1 (0-81.4 μM), decreased in a dose-dependent manner, the fluorescence anisotropy of TMA-DPH (from 0.349 ± 0.003 to 0.1720 ± 0.0035) in dpPC bilayers, whilst no differences were registered with DPH. At 5.6 μM in the subphase, FB1 increased the lateral surface pressure (π) of a Langmuir film to an extent that depended on the monolayer composition (ΔπdpPC:DOTAP 3:1 > ΔπdpPC:dpPA3:1 > ΔπdpPC), the molecular packing (Δπ decreased linearly as a function of the initial π) and the subphase pH (ΔπpH 2.6 > ΔπpH 7.4 and maximal π allowing the drug penetration πcut-off was 34.3 and 27.7 mN/m at pH 2.63 and 7.4, respectively). FB1 increased the surface potential of dpPC and dpPC:DOTAP monolayers and decreased that of dpPC:dpPA. This suggested that FB1 acquired different orientations and/or foldings depending on the surface electrostatics and the toxin charge state. Moreover, FB1-lipid interactions were transduced into long-range effects at the mesoscopic level affecting the lipidic self-separated lateral domains shape and density.
publishDate 2008
dc.date.none.fl_str_mv 2008-06-15
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/11336/57747
Theumer, Martín Gustavo; Clop, Eduardo Matias; Rubinstein, Héctor Ramón; Perillo, Maria Angelica; The lipid-mediated hypothesis of fumonisin B1 toxicodynamics tested in model membranes; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 64; 1; 15-6-2008; 22-33
0927-7765
CONICET Digital
CONICET
url http://hdl.handle.net/11336/57747
identifier_str_mv Theumer, Martín Gustavo; Clop, Eduardo Matias; Rubinstein, Héctor Ramón; Perillo, Maria Angelica; The lipid-mediated hypothesis of fumonisin B1 toxicodynamics tested in model membranes; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 64; 1; 15-6-2008; 22-33
0927-7765
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.sciencedirect.com/science/article/pii/S0927776508000052
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfb.2008.01.002
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
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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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