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 4m 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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/226922
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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 4m 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 Técnicas2025-09-03T09:49:09Zoai: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:34982025-09-03 09:49:09.621CONICET 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 4m 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 4m 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 |
dc.relation.none.fl_str_mv |
info: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. |
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 application/pdf application/pdf |
dc.coverage.none.fl_str_mv |
Nacional |
dc.publisher.none.fl_str_mv |
Sociedad Argentina de Biofísica |
publisher.none.fl_str_mv |
Sociedad Argentina de Biofísica |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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13.13397 |