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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/238527

id CONICETDig_11a98b944ec273e85154c85c623c3cb4
oai_identifier_str oai:ri.conicet.gov.ar:11336/238527
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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
_version_ 1842269856358989824
score 13.13397