Membrane order and ionic strength modulation of the inhibition of the membrane-bound acetylcholinesterase by epigallocatechin‑3‑gallate

Autores
Salazar, Paula Belén; Dupuy, Fernando Gabriel; de Athayde Moncovo Collado, Alejandro; Minahk, Carlos Javier
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In the present work, we analyzed how external factors can modulate the efficiency of epigallocatechin‑3‑O‑gallate (EGCG) inhibition of a membrane-bound isoform of the acetylcholinesterase. Increasing the ionic strength but not the osmolarity of the bulk medium proved to be an important factor. In addition, we verified a clear correlation between the inhibitory activity with the order degree of the membranes by using cholesterol-partially depleted red blood cell ghosts. These two factors i.e. high salt concentration in the bulk medium and less viscous membranes, allow a deeper insertion of the EGCG into the lipid bilayer, thus leading to a greater inhibition of AChE. As a corollary, we propose that any treatment or process that leads to a slight decrease in cholesterol content in the membranes can efficiently enhance the inhibitory activity of EGCG, which can have important consequences in all the pathologies where the inhibition of AChE is recommended.
Fil: Salazar, Paula Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Dupuy, Fernando Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: de Athayde Moncovo Collado, Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Minahk, Carlos Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Materia
IONIC STRENGTH
MEMBRANE INTERACTION
CHOLESTEROL
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:11336/121565
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/121565
network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Membrane order and ionic strength modulation of the inhibition of the membrane-bound acetylcholinesterase by epigallocatechin‑3‑gallateSalazar, Paula BelénDupuy, Fernando Gabrielde Athayde Moncovo Collado, AlejandroMinahk, Carlos JavierIONIC STRENGTHMEMBRANE INTERACTIONCHOLESTEROLhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In the present work, we analyzed how external factors can modulate the efficiency of epigallocatechin‑3‑O‑gallate (EGCG) inhibition of a membrane-bound isoform of the acetylcholinesterase. Increasing the ionic strength but not the osmolarity of the bulk medium proved to be an important factor. In addition, we verified a clear correlation between the inhibitory activity with the order degree of the membranes by using cholesterol-partially depleted red blood cell ghosts. These two factors i.e. high salt concentration in the bulk medium and less viscous membranes, allow a deeper insertion of the EGCG into the lipid bilayer, thus leading to a greater inhibition of AChE. As a corollary, we propose that any treatment or process that leads to a slight decrease in cholesterol content in the membranes can efficiently enhance the inhibitory activity of EGCG, which can have important consequences in all the pathologies where the inhibition of AChE is recommended.Fil: Salazar, Paula Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Dupuy, Fernando Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: de Athayde Moncovo Collado, Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Minahk, Carlos Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaElsevier B.V.2019-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/121565Salazar, Paula Belén; Dupuy, Fernando Gabriel; de Athayde Moncovo Collado, Alejandro; Minahk, Carlos Javier; Membrane order and ionic strength modulation of the inhibition of the membrane-bound acetylcholinesterase by epigallocatechin‑3‑gallate; Elsevier B.V.; Biochimica et Biophysica Acta - Biomembranes; 1861; 1; 8-2019; 170-1770005-27361879-2642CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2018.08.002info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273618302335info:eu-repo/semantics/altIdentifier/url/https://pubmed.ncbi.nlm.nih.gov/30463700/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:27:10Zoai:ri.conicet.gov.ar:11336/121565instacron: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 10:27:10.497CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Membrane order and ionic strength modulation of the inhibition of the membrane-bound acetylcholinesterase by epigallocatechin‑3‑gallate
title Membrane order and ionic strength modulation of the inhibition of the membrane-bound acetylcholinesterase by epigallocatechin‑3‑gallate
spellingShingle Membrane order and ionic strength modulation of the inhibition of the membrane-bound acetylcholinesterase by epigallocatechin‑3‑gallate
Salazar, Paula Belén
IONIC STRENGTH
MEMBRANE INTERACTION
CHOLESTEROL
title_short Membrane order and ionic strength modulation of the inhibition of the membrane-bound acetylcholinesterase by epigallocatechin‑3‑gallate
title_full Membrane order and ionic strength modulation of the inhibition of the membrane-bound acetylcholinesterase by epigallocatechin‑3‑gallate
title_fullStr Membrane order and ionic strength modulation of the inhibition of the membrane-bound acetylcholinesterase by epigallocatechin‑3‑gallate
title_full_unstemmed Membrane order and ionic strength modulation of the inhibition of the membrane-bound acetylcholinesterase by epigallocatechin‑3‑gallate
title_sort Membrane order and ionic strength modulation of the inhibition of the membrane-bound acetylcholinesterase by epigallocatechin‑3‑gallate
dc.creator.none.fl_str_mv Salazar, Paula Belén
Dupuy, Fernando Gabriel
de Athayde Moncovo Collado, Alejandro
Minahk, Carlos Javier
author Salazar, Paula Belén
author_facet Salazar, Paula Belén
Dupuy, Fernando Gabriel
de Athayde Moncovo Collado, Alejandro
Minahk, Carlos Javier
author_role author
author2 Dupuy, Fernando Gabriel
de Athayde Moncovo Collado, Alejandro
Minahk, Carlos Javier
author2_role author
author
author
dc.subject.none.fl_str_mv IONIC STRENGTH
MEMBRANE INTERACTION
CHOLESTEROL
topic IONIC STRENGTH
MEMBRANE INTERACTION
CHOLESTEROL
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv In the present work, we analyzed how external factors can modulate the efficiency of epigallocatechin‑3‑O‑gallate (EGCG) inhibition of a membrane-bound isoform of the acetylcholinesterase. Increasing the ionic strength but not the osmolarity of the bulk medium proved to be an important factor. In addition, we verified a clear correlation between the inhibitory activity with the order degree of the membranes by using cholesterol-partially depleted red blood cell ghosts. These two factors i.e. high salt concentration in the bulk medium and less viscous membranes, allow a deeper insertion of the EGCG into the lipid bilayer, thus leading to a greater inhibition of AChE. As a corollary, we propose that any treatment or process that leads to a slight decrease in cholesterol content in the membranes can efficiently enhance the inhibitory activity of EGCG, which can have important consequences in all the pathologies where the inhibition of AChE is recommended.
Fil: Salazar, Paula Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Dupuy, Fernando Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: de Athayde Moncovo Collado, Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Minahk, Carlos Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
description In the present work, we analyzed how external factors can modulate the efficiency of epigallocatechin‑3‑O‑gallate (EGCG) inhibition of a membrane-bound isoform of the acetylcholinesterase. Increasing the ionic strength but not the osmolarity of the bulk medium proved to be an important factor. In addition, we verified a clear correlation between the inhibitory activity with the order degree of the membranes by using cholesterol-partially depleted red blood cell ghosts. These two factors i.e. high salt concentration in the bulk medium and less viscous membranes, allow a deeper insertion of the EGCG into the lipid bilayer, thus leading to a greater inhibition of AChE. As a corollary, we propose that any treatment or process that leads to a slight decrease in cholesterol content in the membranes can efficiently enhance the inhibitory activity of EGCG, which can have important consequences in all the pathologies where the inhibition of AChE is recommended.
publishDate 2019
dc.date.none.fl_str_mv 2019-08
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/11336/121565
Salazar, Paula Belén; Dupuy, Fernando Gabriel; de Athayde Moncovo Collado, Alejandro; Minahk, Carlos Javier; Membrane order and ionic strength modulation of the inhibition of the membrane-bound acetylcholinesterase by epigallocatechin‑3‑gallate; Elsevier B.V.; Biochimica et Biophysica Acta - Biomembranes; 1861; 1; 8-2019; 170-177
0005-2736
1879-2642
CONICET Digital
CONICET
url http://hdl.handle.net/11336/121565
identifier_str_mv Salazar, Paula Belén; Dupuy, Fernando Gabriel; de Athayde Moncovo Collado, Alejandro; Minahk, Carlos Javier; Membrane order and ionic strength modulation of the inhibition of the membrane-bound acetylcholinesterase by epigallocatechin‑3‑gallate; Elsevier B.V.; Biochimica et Biophysica Acta - Biomembranes; 1861; 1; 8-2019; 170-177
0005-2736
1879-2642
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.2018.08.002
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273618302335
info:eu-repo/semantics/altIdentifier/url/https://pubmed.ncbi.nlm.nih.gov/30463700/
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
dc.publisher.none.fl_str_mv Elsevier B.V.
publisher.none.fl_str_mv Elsevier B.V.
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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