Surface characterization of Langmuir-Blodgett films from bovine erythrocyte membranes (BEM)

Autores
Felsztyna, Iván; Turina, Anahi del Valle; Perillo, Maria Angelica; Clop, Eduardo Matias
Año de publicación
2020
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
This work was aimed at designing an enzyme-based biosensor. So, Langmuir films from bovine erythrocyte membranes (LFBEM) were prepared and transferred to alkylated glasses (Langmuir-Blodgett films, LBBEM). Epifluorescence Microscopy (EFM) and Brewster Angle Microscopy (BAM) were performed on LFBEM. Additionally, EFM and Atomic Force Microscopy (AFM) were performed on LBBEM. The LBBEM was used as the enzyme source for measuring the activity of Bovine Erythrocyte Acetylcholinesterase (BEA).While the rheological behavior of LFBEM was compatible with an expanded monolayer throughout the entire isotherm, in EFM and BAM images, it exhibited a marked topographic heterogeneity which was associated to coexisting fluid domains. Remarkably, in BAM images at   30 mN/m irregular dark regions with reflectivity values similar to the clean interface were found, suggesting the presence of cracks in the film.EFM images of LBBEM roughly conserved the topography of the original LFBEM but with less heterogeneity. The AFM images of LBBEM showed some structures with < 60 nm height, which resembled closed vesicles and when transferred at 35mN/m (a bilayer equilibrium surface pressure) it exhibited a 4m wide depressed regions of 5 nm depth typical of the phase coexistence. Taken together, EFM, BAM and AFM images suggest that over the air-water interface, as well as over the silanized glass substrate, the surface is mostly covered by a monolayer with a few particles dispersed. It is worth to note that BEA present in LBBEM could retain its catalytic activity along several days of storage and maintained the expected kinetic behavior in the presence of some known enzyme modulators.In these systems, the use of natural membranes offers compositional and structural complexity allowing the study of various phenomena of biophysical and cellular interest and facilitates, the building up of biosensors based on the activity of membrane bound enzymes preserving the protein´s natural environment.
Fil: Felsztyna, Iván. 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 Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; Argentina
Fil: Turina, Anahi del Valle. 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 Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; 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 Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; 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 Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; Argentina
Primeras jornadas virtuales de la Sociedad Argentina de Biofísica
Buenos Aires
Argentina
Sociedad Argentina de Biofísica
Materia
Bovine erythrocyte membranes
Bovine erythrocyte acetylcholinesterase
Biosensors
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:11336/226922
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/226922
network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Surface characterization of Langmuir-Blodgett films from bovine erythrocyte membranes (BEM)Felsztyna, IvánTurina, Anahi del VallePerillo, Maria AngelicaClop, Eduardo MatiasBovine erythrocyte membranesBovine erythrocyte acetylcholinesteraseBiosensorshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1This work was aimed at designing an enzyme-based biosensor. So, Langmuir films from bovine erythrocyte membranes (LFBEM) were prepared and transferred to alkylated glasses (Langmuir-Blodgett films, LBBEM). Epifluorescence Microscopy (EFM) and Brewster Angle Microscopy (BAM) were performed on LFBEM. Additionally, EFM and Atomic Force Microscopy (AFM) were performed on LBBEM. The LBBEM was used as the enzyme source for measuring the activity of Bovine Erythrocyte Acetylcholinesterase (BEA).While the rheological behavior of LFBEM was compatible with an expanded monolayer throughout the entire isotherm, in EFM and BAM images, it exhibited a marked topographic heterogeneity which was associated to coexisting fluid domains. Remarkably, in BAM images at   30 mN/m irregular dark regions with reflectivity values similar to the clean interface were found, suggesting the presence of cracks in the film.EFM images of LBBEM roughly conserved the topography of the original LFBEM but with less heterogeneity. The AFM images of LBBEM showed some structures with < 60 nm height, which resembled closed vesicles and when transferred at 35mN/m (a bilayer equilibrium surface pressure) it exhibited a 4m wide depressed regions of 5 nm depth typical of the phase coexistence. Taken together, EFM, BAM and AFM images suggest that over the air-water interface, as well as over the silanized glass substrate, the surface is mostly covered by a monolayer with a few particles dispersed. It is worth to note that BEA present in LBBEM could retain its catalytic activity along several days of storage and maintained the expected kinetic behavior in the presence of some known enzyme modulators.In these systems, the use of natural membranes offers compositional and structural complexity allowing the study of various phenomena of biophysical and cellular interest and facilitates, the building up of biosensors based on the activity of membrane bound enzymes preserving the protein´s natural environment.Fil: Felsztyna, Iván. 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 Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; ArgentinaFil: Turina, Anahi del Valle. 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 Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; 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 Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; 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 Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; ArgentinaPrimeras jornadas virtuales de la Sociedad Argentina de BiofísicaBuenos AiresArgentinaSociedad Argentina de BiofísicaSociedad Argentina de BiofísicaDelfino, Jose MariaCelej, Maria Soledad2020info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectJornadaBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/226922Surface characterization of Langmuir-Blodgett films from bovine erythrocyte membranes (BEM); Primeras jornadas virtuales de la Sociedad Argentina de Biofísica; Buenos Aires; Argentina; 2020; 39-39978-987-27591-8-6CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/reuniones-cientificas/reunionsab-previas/#:~:text=Primeras%20jornadas%20virtuales%20SAB%2C%203,2017%2C%20Buenos%20Aires%2C%20Argentina.Nacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:42:48Zoai:ri.conicet.gov.ar:11336/226922instacron: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 09:42:48.948CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Surface characterization of Langmuir-Blodgett films from bovine erythrocyte membranes (BEM)
title Surface characterization of Langmuir-Blodgett films from bovine erythrocyte membranes (BEM)
spellingShingle Surface characterization of Langmuir-Blodgett films from bovine erythrocyte membranes (BEM)
Felsztyna, Iván
Bovine erythrocyte membranes
Bovine erythrocyte acetylcholinesterase
Biosensors
title_short Surface characterization of Langmuir-Blodgett films from bovine erythrocyte membranes (BEM)
title_full Surface characterization of Langmuir-Blodgett films from bovine erythrocyte membranes (BEM)
title_fullStr Surface characterization of Langmuir-Blodgett films from bovine erythrocyte membranes (BEM)
title_full_unstemmed Surface characterization of Langmuir-Blodgett films from bovine erythrocyte membranes (BEM)
title_sort Surface characterization of Langmuir-Blodgett films from bovine erythrocyte membranes (BEM)
dc.creator.none.fl_str_mv Felsztyna, Iván
Turina, Anahi del Valle
Perillo, Maria Angelica
Clop, Eduardo Matias
author Felsztyna, Iván
author_facet Felsztyna, Iván
Turina, Anahi del Valle
Perillo, Maria Angelica
Clop, Eduardo Matias
author_role author
author2 Turina, Anahi del Valle
Perillo, Maria Angelica
Clop, Eduardo Matias
author2_role author
author
author
dc.contributor.none.fl_str_mv Delfino, Jose Maria
Celej, Maria Soledad
dc.subject.none.fl_str_mv Bovine erythrocyte membranes
Bovine erythrocyte acetylcholinesterase
Biosensors
topic Bovine erythrocyte membranes
Bovine erythrocyte acetylcholinesterase
Biosensors
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv This work was aimed at designing an enzyme-based biosensor. So, Langmuir films from bovine erythrocyte membranes (LFBEM) were prepared and transferred to alkylated glasses (Langmuir-Blodgett films, LBBEM). Epifluorescence Microscopy (EFM) and Brewster Angle Microscopy (BAM) were performed on LFBEM. Additionally, EFM and Atomic Force Microscopy (AFM) were performed on LBBEM. The LBBEM was used as the enzyme source for measuring the activity of Bovine Erythrocyte Acetylcholinesterase (BEA).While the rheological behavior of LFBEM was compatible with an expanded monolayer throughout the entire isotherm, in EFM and BAM images, it exhibited a marked topographic heterogeneity which was associated to coexisting fluid domains. Remarkably, in BAM images at   30 mN/m irregular dark regions with reflectivity values similar to the clean interface were found, suggesting the presence of cracks in the film.EFM images of LBBEM roughly conserved the topography of the original LFBEM but with less heterogeneity. The AFM images of LBBEM showed some structures with < 60 nm height, which resembled closed vesicles and when transferred at 35mN/m (a bilayer equilibrium surface pressure) it exhibited a 4m wide depressed regions of 5 nm depth typical of the phase coexistence. Taken together, EFM, BAM and AFM images suggest that over the air-water interface, as well as over the silanized glass substrate, the surface is mostly covered by a monolayer with a few particles dispersed. It is worth to note that BEA present in LBBEM could retain its catalytic activity along several days of storage and maintained the expected kinetic behavior in the presence of some known enzyme modulators.In these systems, the use of natural membranes offers compositional and structural complexity allowing the study of various phenomena of biophysical and cellular interest and facilitates, the building up of biosensors based on the activity of membrane bound enzymes preserving the protein´s natural environment.
Fil: Felsztyna, Iván. 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 Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; Argentina
Fil: Turina, Anahi del Valle. 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 Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; 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 Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; 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 Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Departamento de Química. Cátedra de Química Biológica; Argentina
Primeras jornadas virtuales de la Sociedad Argentina de Biofísica
Buenos Aires
Argentina
Sociedad Argentina de Biofísica
description This work was aimed at designing an enzyme-based biosensor. So, Langmuir films from bovine erythrocyte membranes (LFBEM) were prepared and transferred to alkylated glasses (Langmuir-Blodgett films, LBBEM). Epifluorescence Microscopy (EFM) and Brewster Angle Microscopy (BAM) were performed on LFBEM. Additionally, EFM and Atomic Force Microscopy (AFM) were performed on LBBEM. The LBBEM was used as the enzyme source for measuring the activity of Bovine Erythrocyte Acetylcholinesterase (BEA).While the rheological behavior of LFBEM was compatible with an expanded monolayer throughout the entire isotherm, in EFM and BAM images, it exhibited a marked topographic heterogeneity which was associated to coexisting fluid domains. Remarkably, in BAM images at   30 mN/m irregular dark regions with reflectivity values similar to the clean interface were found, suggesting the presence of cracks in the film.EFM images of LBBEM roughly conserved the topography of the original LFBEM but with less heterogeneity. The AFM images of LBBEM showed some structures with < 60 nm height, which resembled closed vesicles and when transferred at 35mN/m (a bilayer equilibrium surface pressure) it exhibited a 4m wide depressed regions of 5 nm depth typical of the phase coexistence. Taken together, EFM, BAM and AFM images suggest that over the air-water interface, as well as over the silanized glass substrate, the surface is mostly covered by a monolayer with a few particles dispersed. It is worth to note that BEA present in LBBEM could retain its catalytic activity along several days of storage and maintained the expected kinetic behavior in the presence of some known enzyme modulators.In these systems, the use of natural membranes offers compositional and structural complexity allowing the study of various phenomena of biophysical and cellular interest and facilitates, the building up of biosensors based on the activity of membrane bound enzymes preserving the protein´s natural environment.
publishDate 2020
dc.date.none.fl_str_mv 2020
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Jornada
Book
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/226922
Surface characterization of Langmuir-Blodgett films from bovine erythrocyte membranes (BEM); Primeras jornadas virtuales de la Sociedad Argentina de Biofísica; Buenos Aires; Argentina; 2020; 39-39
978-987-27591-8-6
CONICET Digital
CONICET
url http://hdl.handle.net/11336/226922
identifier_str_mv Surface characterization of Langmuir-Blodgett films from bovine erythrocyte membranes (BEM); Primeras jornadas virtuales de la Sociedad Argentina de Biofísica; Buenos Aires; Argentina; 2020; 39-39
978-987-27591-8-6
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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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/
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application/pdf
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dc.publisher.none.fl_str_mv Sociedad Argentina de Biofísica
publisher.none.fl_str_mv Sociedad Argentina de Biofísica
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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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