Three to Tango: Inhibitory Effect of Quercetin and Apigenin on Acetylcholinesterase, Amyloid-β Aggregation and Acetylcholinesterase-Amyloid Interaction

One of the pathological hallmarks of Alzheimer's disease (AD) is the formation of amyloid-β plaques. Since acetylcholinesterase (AChE) promotes the formation of such plaques, the inhibition of this enzyme could slow down the progression of amyloid-β aggregation, hence being complementary to the...

ver descrição completa

Detalhes bibliográficos
Autores: Alvarez-Berbel, Irene, Espargaró Colomé, Alba, Viayna, Elisabet, Caballero Hernández, Ana Belén, Busquets i Viñas, Ma. Antonia, Gámez Enamorado, Patrick, Luque Garriga, F. Xavier, Sabaté Lagunas, Raimon
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2022
País:España
Recursos:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/192126
Acesso em linha:https://hdl.handle.net/2445/192126
Access Level:acceso abierto
Palavra-chave:Malaltia d'Alzheimer
Pèptids
Amiloïdosi
Alzheimer's disease
Peptides
Amyloidosis
id ES_17cd76ce6dabb54b2f9cb1ce93b3f6cb
oai_identifier_str oai:diposit.ub.edu:2445/192126
network_acronym_str ES
network_name_str España
repository_id_str
spelling Three to Tango: Inhibitory Effect of Quercetin and Apigenin on Acetylcholinesterase, Amyloid-β Aggregation and Acetylcholinesterase-Amyloid InteractionAlvarez-Berbel, IreneEspargaró Colomé, AlbaViayna, ElisabetCaballero Hernández, Ana BelénBusquets i Viñas, Ma. AntoniaGámez Enamorado, PatrickLuque Garriga, F. XavierSabaté Lagunas, RaimonMalaltia d'AlzheimerPèptidsAmiloïdosiAlzheimer's diseasePeptidesAmyloidosisOne of the pathological hallmarks of Alzheimer's disease (AD) is the formation of amyloid-β plaques. Since acetylcholinesterase (AChE) promotes the formation of such plaques, the inhibition of this enzyme could slow down the progression of amyloid-β aggregation, hence being complementary to the palliative treatment of cholinergic decline. Anti-aggregation assays performed for apigenin and quercetin, which are polyphenolic compounds that exhibit inhibitory properties against the formation of amyloid plaques, reveal distinct inhibitory effects of these compounds on Aβ40 aggregation in the presence and absence of AChE. Furthermore, the analysis of the amyloid fibers formed in the presence of these flavonoids suggests that the Aβ40 aggregates present different quaternary structures, viz., smaller molecular assemblies are generated. In agreement with a non-competitive inhibition of AChE, molecular modeling studies indicate that these effects may be due to the binding of apigenin and quercetin at the peripheral binding site of AChE. Since apigenin and quercetin can also reduce the generation of reactive oxygen species, the data achieved suggest that multitarget catechol-type compounds may be used for the simultaneous treatment of various biological hallmarks of AD.MDPI2022info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/192126Articles publicats en revistes (Nutrició, Ciències de l'Alimentació i Gastronomia)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: https://doi.org/10.3390/pharmaceutics14112342Pharmaceutics, 2022, vol. 14, num. 11, p. 2342https://doi.org/10.3390/pharmaceutics14112342cc-by (c) Alvarez-Berbel, Irene et al., 2022https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1921262026-05-27T06:46:51Z
dc.title.none.fl_str_mv Three to Tango: Inhibitory Effect of Quercetin and Apigenin on Acetylcholinesterase, Amyloid-β Aggregation and Acetylcholinesterase-Amyloid Interaction
title Three to Tango: Inhibitory Effect of Quercetin and Apigenin on Acetylcholinesterase, Amyloid-β Aggregation and Acetylcholinesterase-Amyloid Interaction
spellingShingle Three to Tango: Inhibitory Effect of Quercetin and Apigenin on Acetylcholinesterase, Amyloid-β Aggregation and Acetylcholinesterase-Amyloid Interaction
Alvarez-Berbel, Irene
Malaltia d'Alzheimer
Pèptids
Amiloïdosi
Alzheimer's disease
Peptides
Amyloidosis
title_short Three to Tango: Inhibitory Effect of Quercetin and Apigenin on Acetylcholinesterase, Amyloid-β Aggregation and Acetylcholinesterase-Amyloid Interaction
title_full Three to Tango: Inhibitory Effect of Quercetin and Apigenin on Acetylcholinesterase, Amyloid-β Aggregation and Acetylcholinesterase-Amyloid Interaction
title_fullStr Three to Tango: Inhibitory Effect of Quercetin and Apigenin on Acetylcholinesterase, Amyloid-β Aggregation and Acetylcholinesterase-Amyloid Interaction
title_full_unstemmed Three to Tango: Inhibitory Effect of Quercetin and Apigenin on Acetylcholinesterase, Amyloid-β Aggregation and Acetylcholinesterase-Amyloid Interaction
title_sort Three to Tango: Inhibitory Effect of Quercetin and Apigenin on Acetylcholinesterase, Amyloid-β Aggregation and Acetylcholinesterase-Amyloid Interaction
dc.creator.none.fl_str_mv Alvarez-Berbel, Irene
Espargaró Colomé, Alba
Viayna, Elisabet
Caballero Hernández, Ana Belén
Busquets i Viñas, Ma. Antonia
Gámez Enamorado, Patrick
Luque Garriga, F. Xavier
Sabaté Lagunas, Raimon
author Alvarez-Berbel, Irene
author_facet Alvarez-Berbel, Irene
Espargaró Colomé, Alba
Viayna, Elisabet
Caballero Hernández, Ana Belén
Busquets i Viñas, Ma. Antonia
Gámez Enamorado, Patrick
Luque Garriga, F. Xavier
Sabaté Lagunas, Raimon
author_role author
author2 Espargaró Colomé, Alba
Viayna, Elisabet
Caballero Hernández, Ana Belén
Busquets i Viñas, Ma. Antonia
Gámez Enamorado, Patrick
Luque Garriga, F. Xavier
Sabaté Lagunas, Raimon
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Malaltia d'Alzheimer
Pèptids
Amiloïdosi
Alzheimer's disease
Peptides
Amyloidosis
topic Malaltia d'Alzheimer
Pèptids
Amiloïdosi
Alzheimer's disease
Peptides
Amyloidosis
description One of the pathological hallmarks of Alzheimer's disease (AD) is the formation of amyloid-β plaques. Since acetylcholinesterase (AChE) promotes the formation of such plaques, the inhibition of this enzyme could slow down the progression of amyloid-β aggregation, hence being complementary to the palliative treatment of cholinergic decline. Anti-aggregation assays performed for apigenin and quercetin, which are polyphenolic compounds that exhibit inhibitory properties against the formation of amyloid plaques, reveal distinct inhibitory effects of these compounds on Aβ40 aggregation in the presence and absence of AChE. Furthermore, the analysis of the amyloid fibers formed in the presence of these flavonoids suggests that the Aβ40 aggregates present different quaternary structures, viz., smaller molecular assemblies are generated. In agreement with a non-competitive inhibition of AChE, molecular modeling studies indicate that these effects may be due to the binding of apigenin and quercetin at the peripheral binding site of AChE. Since apigenin and quercetin can also reduce the generation of reactive oxygen species, the data achieved suggest that multitarget catechol-type compounds may be used for the simultaneous treatment of various biological hallmarks of AD.
publishDate 2022
dc.date.none.fl_str_mv 2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/192126
url https://hdl.handle.net/2445/192126
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.3390/pharmaceutics14112342
Pharmaceutics, 2022, vol. 14, num. 11, p. 2342
https://doi.org/10.3390/pharmaceutics14112342
dc.rights.none.fl_str_mv cc-by (c) Alvarez-Berbel, Irene et al., 2022
https://creativecommons.org/licenses/by/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Alvarez-Berbel, Irene et al., 2022
https://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv Articles publicats en revistes (Nutrició, Ciències de l'Alimentació i Gastronomia)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869403944705327104
score 15,300719

Registos relacionados