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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/57747
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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 Técnicas2025-09-29T10:06:12Zoai: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:34982025-09-29 10:06:12.432CONICET 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) |
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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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1844613907666173952 |
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13.070432 |