Quercetin induces lipid domain-dependent permeability
Autor(a) principal: | |
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Data de Publicação: | 2022 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.chemphyslip.2021.105160 http://hdl.handle.net/11449/229945 |
Resumo: | Quercetin is a polyphenolic molecule with a broad spectrum of biological activities derived from its antioxidant property. Its mechanism of action has been explained by its binding and/or interference with enzymes, receptors, transporters and signal transduction systems. Since these important mechanisms generally occur in membrane environments, within and through lipid bilayers, investigating the biophysical properties related to the diversity of lipid compositions of cell membranes may be the key to understanding the role of cell membrane in these processes. In this work, we explored the interaction of quercetin with model membranes of different lipid compositions to access the importance of lipid phases and bilayer homogeneity to the action of quercetin and contribute to the understanding of quercetin multiple activities. Analysis of the influence of quercetin on the morphology and permeability of GUVs, the rigidity of LUVs and affinity to these vesicles showed that quercetin strongly partitions to the more homogeneous environments, but significantly permeates and modifies the more heterogeneous where liquid-disordered, liquid-ordered and solid phases coexist. Our findings support the condensing effect of quercetin, which is observed through a significant rigidifying of bilayers containing 40% cholesterol, but much less evidenced when it is reduced to 20% or in its absence. Nevertheless, the presence of sphingomyelin in the ternary system led to a more heterogeneous bilayer with the formation of micrometric and probably also nanometric domains, which coalesce in the presence of quercetin. This observation together with increased permeability points to an insertion effect. |
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Quercetin induces lipid domain-dependent permeabilityCholesterolGiant vesicles microscopyLipid bilayer effectsLipid/water partition coefficientsPhospholipid membranesQuercetinQuercetin is a polyphenolic molecule with a broad spectrum of biological activities derived from its antioxidant property. Its mechanism of action has been explained by its binding and/or interference with enzymes, receptors, transporters and signal transduction systems. Since these important mechanisms generally occur in membrane environments, within and through lipid bilayers, investigating the biophysical properties related to the diversity of lipid compositions of cell membranes may be the key to understanding the role of cell membrane in these processes. In this work, we explored the interaction of quercetin with model membranes of different lipid compositions to access the importance of lipid phases and bilayer homogeneity to the action of quercetin and contribute to the understanding of quercetin multiple activities. Analysis of the influence of quercetin on the morphology and permeability of GUVs, the rigidity of LUVs and affinity to these vesicles showed that quercetin strongly partitions to the more homogeneous environments, but significantly permeates and modifies the more heterogeneous where liquid-disordered, liquid-ordered and solid phases coexist. Our findings support the condensing effect of quercetin, which is observed through a significant rigidifying of bilayers containing 40% cholesterol, but much less evidenced when it is reduced to 20% or in its absence. Nevertheless, the presence of sphingomyelin in the ternary system led to a more heterogeneous bilayer with the formation of micrometric and probably also nanometric domains, which coalesce in the presence of quercetin. This observation together with increased permeability points to an insertion effect.Departamento de Química e Ciências Ambientais Universidade Estadual Paulista (UNESP) Instituto de Biociências Letras e Ciências Exatas (IBILCE), Câmpus São José do Rio PretoDepartamentode Física Universidade Estadual Paulista (UNESP) Instituto de Biociências Letras e Ciências Exatas (IBILCE), Câmpus São José do Rio PretoDepartamento de Química e Ciências Ambientais Universidade Estadual Paulista (UNESP) Instituto de Biociências Letras e Ciências Exatas (IBILCE), Câmpus São José do Rio PretoDepartamentode Física Universidade Estadual Paulista (UNESP) Instituto de Biociências Letras e Ciências Exatas (IBILCE), Câmpus São José do Rio PretoUniversidade Estadual Paulista (UNESP)Leite, Natália Bueno [UNESP]Martins, Danubia Batista [UNESP]Alvares, Dayane S. [UNESP]Cabrera, Marcia Perez dos Santos [UNESP]2022-04-29T08:36:46Z2022-04-29T08:36:46Z2022-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.chemphyslip.2021.105160Chemistry and Physics of Lipids, v. 242.1873-29410009-3084http://hdl.handle.net/11449/22994510.1016/j.chemphyslip.2021.1051602-s2.0-85119903370Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengChemistry and Physics of Lipidsinfo:eu-repo/semantics/openAccess2022-04-29T08:36:46Zoai:repositorio.unesp.br:11449/229945Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462022-04-29T08:36:46Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Quercetin induces lipid domain-dependent permeability |
title |
Quercetin induces lipid domain-dependent permeability |
spellingShingle |
Quercetin induces lipid domain-dependent permeability Leite, Natália Bueno [UNESP] Cholesterol Giant vesicles microscopy Lipid bilayer effects Lipid/water partition coefficients Phospholipid membranes Quercetin |
title_short |
Quercetin induces lipid domain-dependent permeability |
title_full |
Quercetin induces lipid domain-dependent permeability |
title_fullStr |
Quercetin induces lipid domain-dependent permeability |
title_full_unstemmed |
Quercetin induces lipid domain-dependent permeability |
title_sort |
Quercetin induces lipid domain-dependent permeability |
author |
Leite, Natália Bueno [UNESP] |
author_facet |
Leite, Natália Bueno [UNESP] Martins, Danubia Batista [UNESP] Alvares, Dayane S. [UNESP] Cabrera, Marcia Perez dos Santos [UNESP] |
author_role |
author |
author2 |
Martins, Danubia Batista [UNESP] Alvares, Dayane S. [UNESP] Cabrera, Marcia Perez dos Santos [UNESP] |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (UNESP) |
dc.contributor.author.fl_str_mv |
Leite, Natália Bueno [UNESP] Martins, Danubia Batista [UNESP] Alvares, Dayane S. [UNESP] Cabrera, Marcia Perez dos Santos [UNESP] |
dc.subject.por.fl_str_mv |
Cholesterol Giant vesicles microscopy Lipid bilayer effects Lipid/water partition coefficients Phospholipid membranes Quercetin |
topic |
Cholesterol Giant vesicles microscopy Lipid bilayer effects Lipid/water partition coefficients Phospholipid membranes Quercetin |
description |
Quercetin is a polyphenolic molecule with a broad spectrum of biological activities derived from its antioxidant property. Its mechanism of action has been explained by its binding and/or interference with enzymes, receptors, transporters and signal transduction systems. Since these important mechanisms generally occur in membrane environments, within and through lipid bilayers, investigating the biophysical properties related to the diversity of lipid compositions of cell membranes may be the key to understanding the role of cell membrane in these processes. In this work, we explored the interaction of quercetin with model membranes of different lipid compositions to access the importance of lipid phases and bilayer homogeneity to the action of quercetin and contribute to the understanding of quercetin multiple activities. Analysis of the influence of quercetin on the morphology and permeability of GUVs, the rigidity of LUVs and affinity to these vesicles showed that quercetin strongly partitions to the more homogeneous environments, but significantly permeates and modifies the more heterogeneous where liquid-disordered, liquid-ordered and solid phases coexist. Our findings support the condensing effect of quercetin, which is observed through a significant rigidifying of bilayers containing 40% cholesterol, but much less evidenced when it is reduced to 20% or in its absence. Nevertheless, the presence of sphingomyelin in the ternary system led to a more heterogeneous bilayer with the formation of micrometric and probably also nanometric domains, which coalesce in the presence of quercetin. This observation together with increased permeability points to an insertion effect. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-04-29T08:36:46Z 2022-04-29T08:36:46Z 2022-01-01 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.chemphyslip.2021.105160 Chemistry and Physics of Lipids, v. 242. 1873-2941 0009-3084 http://hdl.handle.net/11449/229945 10.1016/j.chemphyslip.2021.105160 2-s2.0-85119903370 |
url |
http://dx.doi.org/10.1016/j.chemphyslip.2021.105160 http://hdl.handle.net/11449/229945 |
identifier_str_mv |
Chemistry and Physics of Lipids, v. 242. 1873-2941 0009-3084 10.1016/j.chemphyslip.2021.105160 2-s2.0-85119903370 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Chemistry and Physics of Lipids |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1799965536473317376 |