Enzyme inhibitory potential of Ligustrum lucidum Aiton berries
Autor(a) principal: | |
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Data de Publicação: | 2019 |
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/10400.11/6552 |
Resumo: | Ligustrum lucidum Aiton and its berries have been used in Chinese traditional medicine for around two thousand years. In the present study, L. lucidium berries harvested in two regions of Portugal were studied. Haemolytic activity and inhibition of oxidative haemolysis as well as the enzyme inhibitory activities (α-amylase enzyme and acetylcholinesterase) were assessed. Results suggest that the different biological activities varied according to the region where samples were collected. Results demonstrated that the sample obtained from region R1 was the most efficient extract for all parameters evaluated, presenting the lowest values of IC50, 10.67 ± 0.46 μg/mL for the inhibition of erythrocyte oxidative haemolysis, 58.28 ± 3.77 μg/mL for the α-amylase enzyme and 67.67 ± 2.10 μg/mL for the acetylcholinesterase inhibition. L. Lucidum berries may be an interesting source of compounds for use in the development of the therapeutic armamentarium for diseases where enzymatic disruption is believed to play a role |
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Enzyme inhibitory potential of Ligustrum lucidum Aiton berriesLigustrum lucidumAiton berriesDiabetesAlzheimer’s diseaseEnzyme inhibitory potentialLigustrum lucidum Aiton and its berries have been used in Chinese traditional medicine for around two thousand years. In the present study, L. lucidium berries harvested in two regions of Portugal were studied. Haemolytic activity and inhibition of oxidative haemolysis as well as the enzyme inhibitory activities (α-amylase enzyme and acetylcholinesterase) were assessed. Results suggest that the different biological activities varied according to the region where samples were collected. Results demonstrated that the sample obtained from region R1 was the most efficient extract for all parameters evaluated, presenting the lowest values of IC50, 10.67 ± 0.46 μg/mL for the inhibition of erythrocyte oxidative haemolysis, 58.28 ± 3.77 μg/mL for the α-amylase enzyme and 67.67 ± 2.10 μg/mL for the acetylcholinesterase inhibition. L. Lucidum berries may be an interesting source of compounds for use in the development of the therapeutic armamentarium for diseases where enzymatic disruption is believed to play a roleRepositório Científico do Instituto Politécnico de Castelo BrancoPaula, VanessaDelgado, TeresaCampos, M.G.Anjos, O.Estevinho, Letícia M.2019-06-20T23:42:49Z20192019-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.11/6552eng10.3390/molecules24071283info: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:RCAAP2024-02-10T01:48:11Zoai:repositorio.ipcb.pt:10400.11/6552Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T16:37:07.663646Repositório 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 |
Enzyme inhibitory potential of Ligustrum lucidum Aiton berries |
title |
Enzyme inhibitory potential of Ligustrum lucidum Aiton berries |
spellingShingle |
Enzyme inhibitory potential of Ligustrum lucidum Aiton berries Paula, Vanessa Ligustrum lucidum Aiton berries Diabetes Alzheimer’s disease Enzyme inhibitory potential |
title_short |
Enzyme inhibitory potential of Ligustrum lucidum Aiton berries |
title_full |
Enzyme inhibitory potential of Ligustrum lucidum Aiton berries |
title_fullStr |
Enzyme inhibitory potential of Ligustrum lucidum Aiton berries |
title_full_unstemmed |
Enzyme inhibitory potential of Ligustrum lucidum Aiton berries |
title_sort |
Enzyme inhibitory potential of Ligustrum lucidum Aiton berries |
author |
Paula, Vanessa |
author_facet |
Paula, Vanessa Delgado, Teresa Campos, M.G. Anjos, O. Estevinho, Letícia M. |
author_role |
author |
author2 |
Delgado, Teresa Campos, M.G. Anjos, O. Estevinho, Letícia M. |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Repositório Científico do Instituto Politécnico de Castelo Branco |
dc.contributor.author.fl_str_mv |
Paula, Vanessa Delgado, Teresa Campos, M.G. Anjos, O. Estevinho, Letícia M. |
dc.subject.por.fl_str_mv |
Ligustrum lucidum Aiton berries Diabetes Alzheimer’s disease Enzyme inhibitory potential |
topic |
Ligustrum lucidum Aiton berries Diabetes Alzheimer’s disease Enzyme inhibitory potential |
description |
Ligustrum lucidum Aiton and its berries have been used in Chinese traditional medicine for around two thousand years. In the present study, L. lucidium berries harvested in two regions of Portugal were studied. Haemolytic activity and inhibition of oxidative haemolysis as well as the enzyme inhibitory activities (α-amylase enzyme and acetylcholinesterase) were assessed. Results suggest that the different biological activities varied according to the region where samples were collected. Results demonstrated that the sample obtained from region R1 was the most efficient extract for all parameters evaluated, presenting the lowest values of IC50, 10.67 ± 0.46 μg/mL for the inhibition of erythrocyte oxidative haemolysis, 58.28 ± 3.77 μg/mL for the α-amylase enzyme and 67.67 ± 2.10 μg/mL for the acetylcholinesterase inhibition. L. Lucidum berries may be an interesting source of compounds for use in the development of the therapeutic armamentarium for diseases where enzymatic disruption is believed to play a role |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-06-20T23:42:49Z 2019 2019-01-01T00:00:00Z |
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/10400.11/6552 |
url |
http://hdl.handle.net/10400.11/6552 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.3390/molecules24071283 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
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 |
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1799130832705683456 |