Antiacetylcholinesterase activity and docking studies with chlorogenic acid, cynarin and arzanol from Helichrysum stoechas (Asteraceae)
Autor(a) principal: | |
---|---|
Data de Publicação: | 2017 |
Outros Autores: | , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.21/7396 |
Resumo: | This work was aimed at the study of the chemical composition in phenolic compounds responsible for the high antiacetylcholinesterase activity of aqueous extracts (decoctions) from Helichrysum stoechas aerial parts. Chlorogenic acid, cynarin, and arzanol were the main components of decoctions, detected by high-performance liquid chromatography with diode-array detection and liquid chromatography-mass spectrometry/mass spectrometry. Flowers and stems/leaves extracts inhibited antiacetylcholinesterase with IC50 values of 260.7 and 654.8 μg/mL, respectively. The biological activity of these extracts was maintained after in vitro gastrointestinal digestion, indicating that the active compounds present in the extracts were not enzymatically modified by the gastrointestinal system used to simulate the digestion. Molecular docking studies with the main components were carried out in order to obtain information, at the molecular level, as to how these compounds access the enzyme’s active site. The docking study showed for the first time that chlorogenic acid, cynarin, and arzanol fit nicely in the antiacetylcholinesterase active site channel, blocking all access to the catalytic triad. This explained the high inhibitory activity determined during in vitro experiments. |
id |
RCAP_a4b18146ec4aae92cac2f0b43c16ca26 |
---|---|
oai_identifier_str |
oai:repositorio.ipl.pt:10400.21/7396 |
network_acronym_str |
RCAP |
network_name_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository_id_str |
7160 |
spelling |
Antiacetylcholinesterase activity and docking studies with chlorogenic acid, cynarin and arzanol from Helichrysum stoechas (Asteraceae)Acetylcholinesterase inhibitionDockingStudiesChromogenic acidCynarinArzanolThis work was aimed at the study of the chemical composition in phenolic compounds responsible for the high antiacetylcholinesterase activity of aqueous extracts (decoctions) from Helichrysum stoechas aerial parts. Chlorogenic acid, cynarin, and arzanol were the main components of decoctions, detected by high-performance liquid chromatography with diode-array detection and liquid chromatography-mass spectrometry/mass spectrometry. Flowers and stems/leaves extracts inhibited antiacetylcholinesterase with IC50 values of 260.7 and 654.8 μg/mL, respectively. The biological activity of these extracts was maintained after in vitro gastrointestinal digestion, indicating that the active compounds present in the extracts were not enzymatically modified by the gastrointestinal system used to simulate the digestion. Molecular docking studies with the main components were carried out in order to obtain information, at the molecular level, as to how these compounds access the enzyme’s active site. The docking study showed for the first time that chlorogenic acid, cynarin, and arzanol fit nicely in the antiacetylcholinesterase active site channel, blocking all access to the catalytic triad. This explained the high inhibitory activity determined during in vitro experiments.SpringerRCIPLSilva, LetíciaRodrigues, Ana M.Ciriani, MarinaFalé, Pedro Luís VieiraTeixeira, VitorMadeira, PauloMachuqueiro, MiguelPacheco, RitaFlorêncio, Maria HelenaAscensão, LiaSerralheiro, Maria Luisa2017-09-28T13:39:43Z2017-072017-07-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.21/7396engSILVA, Letícia [et al] - Antiacetylcholinesterase activity and docking studies with chlorogenic acid, cynarin and arzanol from Helichrysum stoechas (Asteraceae). Medicinal Chemistry Research. ISSN 1054-2523. Vol. 27, N.º 5 (2018), pp. 1558-15581054-2523 (Print) 1554-812010.1007/s00044-018-2159-zmetadata only accessinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-08-03T09:53:25Zoai:repositorio.ipl.pt:10400.21/7396Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:16:21.450797Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Antiacetylcholinesterase activity and docking studies with chlorogenic acid, cynarin and arzanol from Helichrysum stoechas (Asteraceae) |
title |
Antiacetylcholinesterase activity and docking studies with chlorogenic acid, cynarin and arzanol from Helichrysum stoechas (Asteraceae) |
spellingShingle |
Antiacetylcholinesterase activity and docking studies with chlorogenic acid, cynarin and arzanol from Helichrysum stoechas (Asteraceae) Silva, Letícia Acetylcholinesterase inhibition Docking Studies Chromogenic acid Cynarin Arzanol |
title_short |
Antiacetylcholinesterase activity and docking studies with chlorogenic acid, cynarin and arzanol from Helichrysum stoechas (Asteraceae) |
title_full |
Antiacetylcholinesterase activity and docking studies with chlorogenic acid, cynarin and arzanol from Helichrysum stoechas (Asteraceae) |
title_fullStr |
Antiacetylcholinesterase activity and docking studies with chlorogenic acid, cynarin and arzanol from Helichrysum stoechas (Asteraceae) |
title_full_unstemmed |
Antiacetylcholinesterase activity and docking studies with chlorogenic acid, cynarin and arzanol from Helichrysum stoechas (Asteraceae) |
title_sort |
Antiacetylcholinesterase activity and docking studies with chlorogenic acid, cynarin and arzanol from Helichrysum stoechas (Asteraceae) |
author |
Silva, Letícia |
author_facet |
Silva, Letícia Rodrigues, Ana M. Ciriani, Marina Falé, Pedro Luís Vieira Teixeira, Vitor Madeira, Paulo Machuqueiro, Miguel Pacheco, Rita Florêncio, Maria Helena Ascensão, Lia Serralheiro, Maria Luisa |
author_role |
author |
author2 |
Rodrigues, Ana M. Ciriani, Marina Falé, Pedro Luís Vieira Teixeira, Vitor Madeira, Paulo Machuqueiro, Miguel Pacheco, Rita Florêncio, Maria Helena Ascensão, Lia Serralheiro, Maria Luisa |
author2_role |
author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
RCIPL |
dc.contributor.author.fl_str_mv |
Silva, Letícia Rodrigues, Ana M. Ciriani, Marina Falé, Pedro Luís Vieira Teixeira, Vitor Madeira, Paulo Machuqueiro, Miguel Pacheco, Rita Florêncio, Maria Helena Ascensão, Lia Serralheiro, Maria Luisa |
dc.subject.por.fl_str_mv |
Acetylcholinesterase inhibition Docking Studies Chromogenic acid Cynarin Arzanol |
topic |
Acetylcholinesterase inhibition Docking Studies Chromogenic acid Cynarin Arzanol |
description |
This work was aimed at the study of the chemical composition in phenolic compounds responsible for the high antiacetylcholinesterase activity of aqueous extracts (decoctions) from Helichrysum stoechas aerial parts. Chlorogenic acid, cynarin, and arzanol were the main components of decoctions, detected by high-performance liquid chromatography with diode-array detection and liquid chromatography-mass spectrometry/mass spectrometry. Flowers and stems/leaves extracts inhibited antiacetylcholinesterase with IC50 values of 260.7 and 654.8 μg/mL, respectively. The biological activity of these extracts was maintained after in vitro gastrointestinal digestion, indicating that the active compounds present in the extracts were not enzymatically modified by the gastrointestinal system used to simulate the digestion. Molecular docking studies with the main components were carried out in order to obtain information, at the molecular level, as to how these compounds access the enzyme’s active site. The docking study showed for the first time that chlorogenic acid, cynarin, and arzanol fit nicely in the antiacetylcholinesterase active site channel, blocking all access to the catalytic triad. This explained the high inhibitory activity determined during in vitro experiments. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-09-28T13:39:43Z 2017-07 2017-07-01T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.21/7396 |
url |
http://hdl.handle.net/10400.21/7396 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
SILVA, Letícia [et al] - Antiacetylcholinesterase activity and docking studies with chlorogenic acid, cynarin and arzanol from Helichrysum stoechas (Asteraceae). Medicinal Chemistry Research. ISSN 1054-2523. Vol. 27, N.º 5 (2018), pp. 1558-1558 1054-2523 (Print) 1554-8120 10.1007/s00044-018-2159-z |
dc.rights.driver.fl_str_mv |
metadata only access info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
metadata only access |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Springer |
publisher.none.fl_str_mv |
Springer |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
|
_version_ |
1799133423852322816 |