Lysophosphatidylcholine–arbutin complexes form bilayer-like structures

Autores
Frías, María de los Ángeles; Winik, Beatriz Clara; Franzoni, Maria Belen; Levstein, Patricia Rebeca; Nicastro, Alcides; Gennaro, Ana Maria; Díaz, Sonia Beatriz; Disalvo, Edgardo Anibal
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Arbutin is known to suppress melanin production in murine B16 melanoma cells and inhibit phospholipase action. This encourages the possibility to stabilize it in lipid aggregates for its administration in medical applications. Thus, it was of interest to demonstrate that monomyristoylphosphatidylcholine (14:0 lysoPC) and arbutin may form association complexes. This was studied by Electron Microscopy (EM), 31P Nuclear Magnetic Resonance (31P NMR), Electronic Paramagnetic Resonance (EPR) and Fourier Transform Infrared Spectroscopy (FTIR). EM images show the formation of particles of c.a. 6 nm in diameter. For a 1:1 lysoPC–arbutin molar ratio 31P NMR shows a spectrum with a shoulder that resembles the axially symmetric spectrum characteristic of vesicles. The addition of La3+ ions to the arbutin–lysoPC complex allows one to distinguish two phosphorous populations. These results suggest that arbutin–lysoPC forms vesicles with bilayers stabilized in an interdigitated array. FTIR spectroscopy shows that arbutin interacts with the hydrated population of the carbonyl groups and with the phosphates through the formation of hydrogen bonds. It is interpreted that hydrophobic interactions among the phenol group of arbutin and the acyl chain of lysoPC are responsible for the decrease in acyl chain mobility observed at the 5th C level by EPR. A model proposing the formation of interdigitated bilayers of arbutin-lysoPC could explain the experimental results.
Fil: Frías, María de los Ángeles. Universidad Nacional de Tucuman. Facultad de Bioquímica, Química y Farmacia. Instituto de Química Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Winik, Beatriz Clara. Universidad Nacional de Tucumán; Argentina
Fil: Franzoni, Maria Belen. Universidad Nacional de Córdoba. Facultad de Matemática, Astronomía y Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Levstein, Patricia Rebeca. Universidad Nacional de Córdoba. Facultad de Matemática, Astronomía y Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Nicastro, Alcides. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
Fil: Gennaro, Ana Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
Fil: Díaz, Sonia Beatriz. Universidad Nacional de Tucuman. Facultad de Bioquímica, Química y Farmacia. Instituto de Química Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Disalvo, Edgardo Anibal. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Lysopc
Arbutin
Interdigitation
Ftir Interactions
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/25191
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/25191
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Lysophosphatidylcholine–arbutin complexes form bilayer-like structuresFrías, María de los ÁngelesWinik, Beatriz ClaraFranzoni, Maria BelenLevstein, Patricia RebecaNicastro, AlcidesGennaro, Ana MariaDíaz, Sonia BeatrizDisalvo, Edgardo AnibalLysopcArbutinInterdigitationFtir Interactionshttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Arbutin is known to suppress melanin production in murine B16 melanoma cells and inhibit phospholipase action. This encourages the possibility to stabilize it in lipid aggregates for its administration in medical applications. Thus, it was of interest to demonstrate that monomyristoylphosphatidylcholine (14:0 lysoPC) and arbutin may form association complexes. This was studied by Electron Microscopy (EM), 31P Nuclear Magnetic Resonance (31P NMR), Electronic Paramagnetic Resonance (EPR) and Fourier Transform Infrared Spectroscopy (FTIR). EM images show the formation of particles of c.a. 6 nm in diameter. For a 1:1 lysoPC–arbutin molar ratio 31P NMR shows a spectrum with a shoulder that resembles the axially symmetric spectrum characteristic of vesicles. The addition of La3+ ions to the arbutin–lysoPC complex allows one to distinguish two phosphorous populations. These results suggest that arbutin–lysoPC forms vesicles with bilayers stabilized in an interdigitated array. FTIR spectroscopy shows that arbutin interacts with the hydrated population of the carbonyl groups and with the phosphates through the formation of hydrogen bonds. It is interpreted that hydrophobic interactions among the phenol group of arbutin and the acyl chain of lysoPC are responsible for the decrease in acyl chain mobility observed at the 5th C level by EPR. A model proposing the formation of interdigitated bilayers of arbutin-lysoPC could explain the experimental results.Fil: Frías, María de los Ángeles. Universidad Nacional de Tucuman. Facultad de Bioquímica, Química y Farmacia. Instituto de Química Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Winik, Beatriz Clara. Universidad Nacional de Tucumán; ArgentinaFil: Franzoni, Maria Belen. Universidad Nacional de Córdoba. Facultad de Matemática, Astronomía y Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Levstein, Patricia Rebeca. Universidad Nacional de Córdoba. Facultad de Matemática, Astronomía y Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Nicastro, Alcides. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; ArgentinaFil: Gennaro, Ana Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; ArgentinaFil: Díaz, Sonia Beatriz. Universidad Nacional de Tucuman. Facultad de Bioquímica, Química y Farmacia. Instituto de Química Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Disalvo, Edgardo Anibal. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier Science2008-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/25191Frías, María de los Ángeles; Winik, Beatriz Clara; Franzoni, Maria Belen; Levstein, Patricia Rebeca; Nicastro, Alcides; et al.; Lysophosphatidylcholine–arbutin complexes form bilayer-like structures; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1778; 5; 2-2008; 1256-12660005-2736CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2008.02.002info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273608000734info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:02:48Zoai:ri.conicet.gov.ar:11336/25191instacron: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 10:02:49.015CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Lysophosphatidylcholine–arbutin complexes form bilayer-like structures
title Lysophosphatidylcholine–arbutin complexes form bilayer-like structures
spellingShingle Lysophosphatidylcholine–arbutin complexes form bilayer-like structures
Frías, María de los Ángeles
Lysopc
Arbutin
Interdigitation
Ftir Interactions
title_short Lysophosphatidylcholine–arbutin complexes form bilayer-like structures
title_full Lysophosphatidylcholine–arbutin complexes form bilayer-like structures
title_fullStr Lysophosphatidylcholine–arbutin complexes form bilayer-like structures
title_full_unstemmed Lysophosphatidylcholine–arbutin complexes form bilayer-like structures
title_sort Lysophosphatidylcholine–arbutin complexes form bilayer-like structures
dc.creator.none.fl_str_mv Frías, María de los Ángeles
Winik, Beatriz Clara
Franzoni, Maria Belen
Levstein, Patricia Rebeca
Nicastro, Alcides
Gennaro, Ana Maria
Díaz, Sonia Beatriz
Disalvo, Edgardo Anibal
author Frías, María de los Ángeles
author_facet Frías, María de los Ángeles
Winik, Beatriz Clara
Franzoni, Maria Belen
Levstein, Patricia Rebeca
Nicastro, Alcides
Gennaro, Ana Maria
Díaz, Sonia Beatriz
Disalvo, Edgardo Anibal
author_role author
author2 Winik, Beatriz Clara
Franzoni, Maria Belen
Levstein, Patricia Rebeca
Nicastro, Alcides
Gennaro, Ana Maria
Díaz, Sonia Beatriz
Disalvo, Edgardo Anibal
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Lysopc
Arbutin
Interdigitation
Ftir Interactions
topic Lysopc
Arbutin
Interdigitation
Ftir Interactions
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Arbutin is known to suppress melanin production in murine B16 melanoma cells and inhibit phospholipase action. This encourages the possibility to stabilize it in lipid aggregates for its administration in medical applications. Thus, it was of interest to demonstrate that monomyristoylphosphatidylcholine (14:0 lysoPC) and arbutin may form association complexes. This was studied by Electron Microscopy (EM), 31P Nuclear Magnetic Resonance (31P NMR), Electronic Paramagnetic Resonance (EPR) and Fourier Transform Infrared Spectroscopy (FTIR). EM images show the formation of particles of c.a. 6 nm in diameter. For a 1:1 lysoPC–arbutin molar ratio 31P NMR shows a spectrum with a shoulder that resembles the axially symmetric spectrum characteristic of vesicles. The addition of La3+ ions to the arbutin–lysoPC complex allows one to distinguish two phosphorous populations. These results suggest that arbutin–lysoPC forms vesicles with bilayers stabilized in an interdigitated array. FTIR spectroscopy shows that arbutin interacts with the hydrated population of the carbonyl groups and with the phosphates through the formation of hydrogen bonds. It is interpreted that hydrophobic interactions among the phenol group of arbutin and the acyl chain of lysoPC are responsible for the decrease in acyl chain mobility observed at the 5th C level by EPR. A model proposing the formation of interdigitated bilayers of arbutin-lysoPC could explain the experimental results.
Fil: Frías, María de los Ángeles. Universidad Nacional de Tucuman. Facultad de Bioquímica, Química y Farmacia. Instituto de Química Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Winik, Beatriz Clara. Universidad Nacional de Tucumán; Argentina
Fil: Franzoni, Maria Belen. Universidad Nacional de Córdoba. Facultad de Matemática, Astronomía y Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Levstein, Patricia Rebeca. Universidad Nacional de Córdoba. Facultad de Matemática, Astronomía y Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Nicastro, Alcides. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
Fil: Gennaro, Ana Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química. Universidad Nacional del Litoral. Instituto de Desarrollo Tecnológico para la Industria Química; Argentina
Fil: Díaz, Sonia Beatriz. Universidad Nacional de Tucuman. Facultad de Bioquímica, Química y Farmacia. Instituto de Química Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Disalvo, Edgardo Anibal. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Arbutin is known to suppress melanin production in murine B16 melanoma cells and inhibit phospholipase action. This encourages the possibility to stabilize it in lipid aggregates for its administration in medical applications. Thus, it was of interest to demonstrate that monomyristoylphosphatidylcholine (14:0 lysoPC) and arbutin may form association complexes. This was studied by Electron Microscopy (EM), 31P Nuclear Magnetic Resonance (31P NMR), Electronic Paramagnetic Resonance (EPR) and Fourier Transform Infrared Spectroscopy (FTIR). EM images show the formation of particles of c.a. 6 nm in diameter. For a 1:1 lysoPC–arbutin molar ratio 31P NMR shows a spectrum with a shoulder that resembles the axially symmetric spectrum characteristic of vesicles. The addition of La3+ ions to the arbutin–lysoPC complex allows one to distinguish two phosphorous populations. These results suggest that arbutin–lysoPC forms vesicles with bilayers stabilized in an interdigitated array. FTIR spectroscopy shows that arbutin interacts with the hydrated population of the carbonyl groups and with the phosphates through the formation of hydrogen bonds. It is interpreted that hydrophobic interactions among the phenol group of arbutin and the acyl chain of lysoPC are responsible for the decrease in acyl chain mobility observed at the 5th C level by EPR. A model proposing the formation of interdigitated bilayers of arbutin-lysoPC could explain the experimental results.
publishDate 2008
dc.date.none.fl_str_mv 2008-02
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/11336/25191
Frías, María de los Ángeles; Winik, Beatriz Clara; Franzoni, Maria Belen; Levstein, Patricia Rebeca; Nicastro, Alcides; et al.; Lysophosphatidylcholine–arbutin complexes form bilayer-like structures; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1778; 5; 2-2008; 1256-1266
0005-2736
CONICET Digital
CONICET
url http://hdl.handle.net/11336/25191
identifier_str_mv Frías, María de los Ángeles; Winik, Beatriz Clara; Franzoni, Maria Belen; Levstein, Patricia Rebeca; Nicastro, Alcides; et al.; Lysophosphatidylcholine–arbutin complexes form bilayer-like structures; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1778; 5; 2-2008; 1256-1266
0005-2736
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2008.02.002
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273608000734
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
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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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score 13.070432

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