Effect of natural terpenes on Bovine erythrocyte acetylcholinesterase (BEA) activity from bovine erythrocyte ghost membranes (BEM): Possible unspecific mechanism that tunes the BEA...
- Autores
- Dutto, Jorge; Turina, Anahi del Valle; Perillo, Maria Angelica; Clop, Eduardo Matias
- Año de publicación
- 2019
- Idioma
- inglés
- Tipo de recurso
- documento de conferencia
- Estado
- versión publicada
- Descripción
- BEA is a GPI-anchored enzyme that hydrolyzessericacetylcholine. The ‘anionic’ subsite in the active site determines the specificity with respect to the choline moiety through electrostatic interactions. Since a) changes on the molecular environment of GPI-anchored enzymes affect their kinetic parameters and b) monoterpenes (MT) affects biomembrane order and electrostatics according to their dipole moment modulus and orientation, here we tested the effects of MTs (1-8 cineol, CIN and camphor, CAM) on the hydrolysis of acethylthiocholine (ATC, Ellman's method)catalyzed by BEA present in BEM. The affinity of the BEA-ATC complex in the absence of MTs (KM=0.1) was significantly affected by CIN which resulted a stronger inhibitor (KM= 0.81) than CAM (KM=0.11) (both at 0.3mM). Moreover, CIN exhibited an IC50=0.3mM whereas the IC50 of CAM was >> 0.6 mM.Measurements of the fluorescence anisotropy (A) of DPH and TMA-DPH in BEM, demonstrated that both MTs affected the organization of the inner regions of the bilayer (both MTs reduced about a 10% the ADPH ) but not the polar head group region (ATMA-DPH was almost unaffected). The effect of MTs on the lateral pressure (π) and surface potential (DV) vs Area compression isotherms in Langmuir films were also studied. In the presence of CIN, the transition found in the control π-Aisotherm become less cooperative and the πcollapse decreased. At low π, the slopes of both isotherms (π-A and DV-A) changed; e.g.we found a DDV~20mV with respect to the control without CIN. At high π,CIN and control isotherms convergedsuggesting the CINmolecules expulsion from the film upon compression. CAM did not produce significant effects on DV, but expanded slightly the whole π-A isotherm up to the collapse point. Concluding, the inhibitory activity of CIN on BEA may be related with its effect on the membrane order and electrostatics which may be interfering unspecificallywith the BEA-ATC electrostatic interaction at the active site.
Fil: Dutto, Jorge. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales; 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
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
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
VII Reunión Científica del IIByT (CONICET-UNC)
Córdoba
Argentina
Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bilógicas y Tecnológicas - Materia
-
GPI-anchored enzyme
Bovine erythrocyte acetylcholinesterase
Langmuir-Schaefer
Terpens - 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:11336/238527
Ver los metadatos del registro completo
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oai:ri.conicet.gov.ar:11336/238527 |
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3498 |
network_name_str |
CONICET Digital (CONICET) |
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Effect of natural terpenes on Bovine erythrocyte acetylcholinesterase (BEA) activity from bovine erythrocyte ghost membranes (BEM): Possible unspecific mechanism that tunes the BEA catalytic activityDutto, JorgeTurina, Anahi del VallePerillo, Maria AngelicaClop, Eduardo MatiasGPI-anchored enzymeBovine erythrocyte acetylcholinesteraseLangmuir-SchaeferTerpenshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1BEA is a GPI-anchored enzyme that hydrolyzessericacetylcholine. The ‘anionic’ subsite in the active site determines the specificity with respect to the choline moiety through electrostatic interactions. Since a) changes on the molecular environment of GPI-anchored enzymes affect their kinetic parameters and b) monoterpenes (MT) affects biomembrane order and electrostatics according to their dipole moment modulus and orientation, here we tested the effects of MTs (1-8 cineol, CIN and camphor, CAM) on the hydrolysis of acethylthiocholine (ATC, Ellman's method)catalyzed by BEA present in BEM. The affinity of the BEA-ATC complex in the absence of MTs (KM=0.1) was significantly affected by CIN which resulted a stronger inhibitor (KM= 0.81) than CAM (KM=0.11) (both at 0.3mM). Moreover, CIN exhibited an IC50=0.3mM whereas the IC50 of CAM was >> 0.6 mM.Measurements of the fluorescence anisotropy (A) of DPH and TMA-DPH in BEM, demonstrated that both MTs affected the organization of the inner regions of the bilayer (both MTs reduced about a 10% the ADPH ) but not the polar head group region (ATMA-DPH was almost unaffected). The effect of MTs on the lateral pressure (π) and surface potential (DV) vs Area compression isotherms in Langmuir films were also studied. In the presence of CIN, the transition found in the control π-Aisotherm become less cooperative and the πcollapse decreased. At low π, the slopes of both isotherms (π-A and DV-A) changed; e.g.we found a DDV~20mV with respect to the control without CIN. At high π,CIN and control isotherms convergedsuggesting the CINmolecules expulsion from the film upon compression. CAM did not produce significant effects on DV, but expanded slightly the whole π-A isotherm up to the collapse point. Concluding, the inhibitory activity of CIN on BEA may be related with its effect on the membrane order and electrostatics which may be interfering unspecificallywith the BEA-ATC electrostatic interaction at the active site.Fil: Dutto, Jorge. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales; 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; 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; 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; ArgentinaVII Reunión Científica del IIByT (CONICET-UNC)CórdobaArgentinaConsejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bilógicas y TecnológicasConsejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bilógicas y TecnológicasMiguel, VirginiaFilippini, Edith Raquel2019info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/238527Effect of natural terpenes on Bovine erythrocyte acetylcholinesterase (BEA) activity from bovine erythrocyte ghost membranes (BEM): Possible unspecific mechanism that tunes the BEA catalytic activity; VII Reunión Científica del IIByT (CONICET-UNC); Córdoba; Argentina; 2019; 13-13CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.iibyt.conicet.unc.edu.ar/files/libro-resumenes-IIByT-2019.pdfinfo:eu-repo/semantics/altIdentifier/url/https://www.iibyt.conicet.unc.edu.ar/reuniones-cientificas-anuales/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 Técnicas2025-09-03T10:04:28Zoai:ri.conicet.gov.ar:11336/238527instacron: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 10:04:28.346CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Effect of natural terpenes on Bovine erythrocyte acetylcholinesterase (BEA) activity from bovine erythrocyte ghost membranes (BEM): Possible unspecific mechanism that tunes the BEA catalytic activity |
title |
Effect of natural terpenes on Bovine erythrocyte acetylcholinesterase (BEA) activity from bovine erythrocyte ghost membranes (BEM): Possible unspecific mechanism that tunes the BEA catalytic activity |
spellingShingle |
Effect of natural terpenes on Bovine erythrocyte acetylcholinesterase (BEA) activity from bovine erythrocyte ghost membranes (BEM): Possible unspecific mechanism that tunes the BEA catalytic activity Dutto, Jorge GPI-anchored enzyme Bovine erythrocyte acetylcholinesterase Langmuir-Schaefer Terpens |
title_short |
Effect of natural terpenes on Bovine erythrocyte acetylcholinesterase (BEA) activity from bovine erythrocyte ghost membranes (BEM): Possible unspecific mechanism that tunes the BEA catalytic activity |
title_full |
Effect of natural terpenes on Bovine erythrocyte acetylcholinesterase (BEA) activity from bovine erythrocyte ghost membranes (BEM): Possible unspecific mechanism that tunes the BEA catalytic activity |
title_fullStr |
Effect of natural terpenes on Bovine erythrocyte acetylcholinesterase (BEA) activity from bovine erythrocyte ghost membranes (BEM): Possible unspecific mechanism that tunes the BEA catalytic activity |
title_full_unstemmed |
Effect of natural terpenes on Bovine erythrocyte acetylcholinesterase (BEA) activity from bovine erythrocyte ghost membranes (BEM): Possible unspecific mechanism that tunes the BEA catalytic activity |
title_sort |
Effect of natural terpenes on Bovine erythrocyte acetylcholinesterase (BEA) activity from bovine erythrocyte ghost membranes (BEM): Possible unspecific mechanism that tunes the BEA catalytic activity |
dc.creator.none.fl_str_mv |
Dutto, Jorge Turina, Anahi del Valle Perillo, Maria Angelica Clop, Eduardo Matias |
author |
Dutto, Jorge |
author_facet |
Dutto, Jorge 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 |
Miguel, Virginia Filippini, Edith Raquel |
dc.subject.none.fl_str_mv |
GPI-anchored enzyme Bovine erythrocyte acetylcholinesterase Langmuir-Schaefer Terpens |
topic |
GPI-anchored enzyme Bovine erythrocyte acetylcholinesterase Langmuir-Schaefer Terpens |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
BEA is a GPI-anchored enzyme that hydrolyzessericacetylcholine. The ‘anionic’ subsite in the active site determines the specificity with respect to the choline moiety through electrostatic interactions. Since a) changes on the molecular environment of GPI-anchored enzymes affect their kinetic parameters and b) monoterpenes (MT) affects biomembrane order and electrostatics according to their dipole moment modulus and orientation, here we tested the effects of MTs (1-8 cineol, CIN and camphor, CAM) on the hydrolysis of acethylthiocholine (ATC, Ellman's method)catalyzed by BEA present in BEM. The affinity of the BEA-ATC complex in the absence of MTs (KM=0.1) was significantly affected by CIN which resulted a stronger inhibitor (KM= 0.81) than CAM (KM=0.11) (both at 0.3mM). Moreover, CIN exhibited an IC50=0.3mM whereas the IC50 of CAM was >> 0.6 mM.Measurements of the fluorescence anisotropy (A) of DPH and TMA-DPH in BEM, demonstrated that both MTs affected the organization of the inner regions of the bilayer (both MTs reduced about a 10% the ADPH ) but not the polar head group region (ATMA-DPH was almost unaffected). The effect of MTs on the lateral pressure (π) and surface potential (DV) vs Area compression isotherms in Langmuir films were also studied. In the presence of CIN, the transition found in the control π-Aisotherm become less cooperative and the πcollapse decreased. At low π, the slopes of both isotherms (π-A and DV-A) changed; e.g.we found a DDV~20mV with respect to the control without CIN. At high π,CIN and control isotherms convergedsuggesting the CINmolecules expulsion from the film upon compression. CAM did not produce significant effects on DV, but expanded slightly the whole π-A isotherm up to the collapse point. Concluding, the inhibitory activity of CIN on BEA may be related with its effect on the membrane order and electrostatics which may be interfering unspecificallywith the BEA-ATC electrostatic interaction at the active site. Fil: Dutto, Jorge. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales; 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 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 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 VII Reunión Científica del IIByT (CONICET-UNC) Córdoba Argentina Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bilógicas y Tecnológicas |
description |
BEA is a GPI-anchored enzyme that hydrolyzessericacetylcholine. The ‘anionic’ subsite in the active site determines the specificity with respect to the choline moiety through electrostatic interactions. Since a) changes on the molecular environment of GPI-anchored enzymes affect their kinetic parameters and b) monoterpenes (MT) affects biomembrane order and electrostatics according to their dipole moment modulus and orientation, here we tested the effects of MTs (1-8 cineol, CIN and camphor, CAM) on the hydrolysis of acethylthiocholine (ATC, Ellman's method)catalyzed by BEA present in BEM. The affinity of the BEA-ATC complex in the absence of MTs (KM=0.1) was significantly affected by CIN which resulted a stronger inhibitor (KM= 0.81) than CAM (KM=0.11) (both at 0.3mM). Moreover, CIN exhibited an IC50=0.3mM whereas the IC50 of CAM was >> 0.6 mM.Measurements of the fluorescence anisotropy (A) of DPH and TMA-DPH in BEM, demonstrated that both MTs affected the organization of the inner regions of the bilayer (both MTs reduced about a 10% the ADPH ) but not the polar head group region (ATMA-DPH was almost unaffected). The effect of MTs on the lateral pressure (π) and surface potential (DV) vs Area compression isotherms in Langmuir films were also studied. In the presence of CIN, the transition found in the control π-Aisotherm become less cooperative and the πcollapse decreased. At low π, the slopes of both isotherms (π-A and DV-A) changed; e.g.we found a DDV~20mV with respect to the control without CIN. At high π,CIN and control isotherms convergedsuggesting the CINmolecules expulsion from the film upon compression. CAM did not produce significant effects on DV, but expanded slightly the whole π-A isotherm up to the collapse point. Concluding, the inhibitory activity of CIN on BEA may be related with its effect on the membrane order and electrostatics which may be interfering unspecificallywith the BEA-ATC electrostatic interaction at the active site. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/conferenceObject Reunión 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/11336/238527 Effect of natural terpenes on Bovine erythrocyte acetylcholinesterase (BEA) activity from bovine erythrocyte ghost membranes (BEM): Possible unspecific mechanism that tunes the BEA catalytic activity; VII Reunión Científica del IIByT (CONICET-UNC); Córdoba; Argentina; 2019; 13-13 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/238527 |
identifier_str_mv |
Effect of natural terpenes on Bovine erythrocyte acetylcholinesterase (BEA) activity from bovine erythrocyte ghost membranes (BEM): Possible unspecific mechanism that tunes the BEA catalytic activity; VII Reunión Científica del IIByT (CONICET-UNC); Córdoba; Argentina; 2019; 13-13 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.iibyt.conicet.unc.edu.ar/files/libro-resumenes-IIByT-2019.pdf info:eu-repo/semantics/altIdentifier/url/https://www.iibyt.conicet.unc.edu.ar/reuniones-cientificas-anuales/ |
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 |
dc.coverage.none.fl_str_mv |
Nacional |
dc.publisher.none.fl_str_mv |
Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bilógicas y Tecnológicas |
publisher.none.fl_str_mv |
Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones Bilógicas y Tecnológicas |
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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1842269856358989824 |
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13.13397 |