Serum albumin modulates the bioactivity of rosmarinic acid
Autor(a) principal: | |
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Data de Publicação: | 2018 |
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/10400.21/11350 |
Resumo: | Rosmarinic acid (RA) is a phenolic compound with biological activity. The objective of the present study was to investigate whether this compound kept its biological activity in the presence of proteins. For this purpose, bovine serum albumin (BSA) was used as a model protein, and the capacity of the RA to inhibit acetylcholinesterase (AChE) and affect antioxidant activity was evaluated in the absence and presence of BSA. A mixture of phenolic compounds containing RA, obtained from a medicinal plant was added to this study. The AChE inhibitory activity of RA was reduced by *57% in the presence of BSA, while the antioxidant activity increased. These results lead to the investigation of the effect of RA on the BSA structure using Fourier transform infrared spectroscopy (FTIR). At 37 C and higher temperatures, RA caused a decrease in the temperature modifications onthe proteinstructure. Furthermore, FTIR and native-gel analysis revealed that protein aggregation/ precipitation, induced bytemperature, wasreduced in thepresence of RA. The novelty of the present work resides in thestudy of the enzyme inhibitory activity and antioxidant capacity of polyphenols, such as RA, in the presence of a protein. The findings highlight the need to consider the presence of proteins when assessing biological activities of polyphenols in vitro and that enzyme inhibitory activity may be decreased, while the antioxidant capacity remains or even increases. |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Serum albumin modulates the bioactivity of rosmarinic acidAcetylcholinesteraseAntioxidant activityFTIRProtein secondary structureSDS-PAGERosmarinic acid (RA) is a phenolic compound with biological activity. The objective of the present study was to investigate whether this compound kept its biological activity in the presence of proteins. For this purpose, bovine serum albumin (BSA) was used as a model protein, and the capacity of the RA to inhibit acetylcholinesterase (AChE) and affect antioxidant activity was evaluated in the absence and presence of BSA. A mixture of phenolic compounds containing RA, obtained from a medicinal plant was added to this study. The AChE inhibitory activity of RA was reduced by *57% in the presence of BSA, while the antioxidant activity increased. These results lead to the investigation of the effect of RA on the BSA structure using Fourier transform infrared spectroscopy (FTIR). At 37 C and higher temperatures, RA caused a decrease in the temperature modifications onthe proteinstructure. Furthermore, FTIR and native-gel analysis revealed that protein aggregation/ precipitation, induced bytemperature, wasreduced in thepresence of RA. The novelty of the present work resides in thestudy of the enzyme inhibitory activity and antioxidant capacity of polyphenols, such as RA, in the presence of a protein. The findings highlight the need to consider the presence of proteins when assessing biological activities of polyphenols in vitro and that enzyme inhibitory activity may be decreased, while the antioxidant capacity remains or even increases.Mary Ann LiebertRCIPLBrito, ElsaSilva, AndréFale, PedroPacheco, RitaSerralheiro, AntónioHaris, Parvez I.Ascensão, LiaSerralheiro, Maria Luisa2020-03-26T18:21:16Z2018-082018-08-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.21/11350engBRITO, Elsa; [et al] – Serum albumin modulates the bioactivity of rosmarinic acid. Journal of Medicinal Food. ISSN 1096-620X. Vol. 21, N.º 8 (2018), pp. 801-8071096-620X.10.1089/jmf.2017.0086metadata 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:RCAAP2023-08-03T10:02:31Zoai:repositorio.ipl.pt:10400.21/11350Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:19:37.157399Repositório 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 |
Serum albumin modulates the bioactivity of rosmarinic acid |
title |
Serum albumin modulates the bioactivity of rosmarinic acid |
spellingShingle |
Serum albumin modulates the bioactivity of rosmarinic acid Brito, Elsa Acetylcholinesterase Antioxidant activity FTIR Protein secondary structure SDS-PAGE |
title_short |
Serum albumin modulates the bioactivity of rosmarinic acid |
title_full |
Serum albumin modulates the bioactivity of rosmarinic acid |
title_fullStr |
Serum albumin modulates the bioactivity of rosmarinic acid |
title_full_unstemmed |
Serum albumin modulates the bioactivity of rosmarinic acid |
title_sort |
Serum albumin modulates the bioactivity of rosmarinic acid |
author |
Brito, Elsa |
author_facet |
Brito, Elsa Silva, André Fale, Pedro Pacheco, Rita Serralheiro, António Haris, Parvez I. Ascensão, Lia Serralheiro, Maria Luisa |
author_role |
author |
author2 |
Silva, André Fale, Pedro Pacheco, Rita Serralheiro, António Haris, Parvez I. Ascensão, Lia Serralheiro, Maria Luisa |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
RCIPL |
dc.contributor.author.fl_str_mv |
Brito, Elsa Silva, André Fale, Pedro Pacheco, Rita Serralheiro, António Haris, Parvez I. Ascensão, Lia Serralheiro, Maria Luisa |
dc.subject.por.fl_str_mv |
Acetylcholinesterase Antioxidant activity FTIR Protein secondary structure SDS-PAGE |
topic |
Acetylcholinesterase Antioxidant activity FTIR Protein secondary structure SDS-PAGE |
description |
Rosmarinic acid (RA) is a phenolic compound with biological activity. The objective of the present study was to investigate whether this compound kept its biological activity in the presence of proteins. For this purpose, bovine serum albumin (BSA) was used as a model protein, and the capacity of the RA to inhibit acetylcholinesterase (AChE) and affect antioxidant activity was evaluated in the absence and presence of BSA. A mixture of phenolic compounds containing RA, obtained from a medicinal plant was added to this study. The AChE inhibitory activity of RA was reduced by *57% in the presence of BSA, while the antioxidant activity increased. These results lead to the investigation of the effect of RA on the BSA structure using Fourier transform infrared spectroscopy (FTIR). At 37 C and higher temperatures, RA caused a decrease in the temperature modifications onthe proteinstructure. Furthermore, FTIR and native-gel analysis revealed that protein aggregation/ precipitation, induced bytemperature, wasreduced in thepresence of RA. The novelty of the present work resides in thestudy of the enzyme inhibitory activity and antioxidant capacity of polyphenols, such as RA, in the presence of a protein. The findings highlight the need to consider the presence of proteins when assessing biological activities of polyphenols in vitro and that enzyme inhibitory activity may be decreased, while the antioxidant capacity remains or even increases. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-08 2018-08-01T00:00:00Z 2020-03-26T18:21:16Z |
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/10400.21/11350 |
url |
http://hdl.handle.net/10400.21/11350 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
BRITO, Elsa; [et al] – Serum albumin modulates the bioactivity of rosmarinic acid. Journal of Medicinal Food. ISSN 1096-620X. Vol. 21, N.º 8 (2018), pp. 801-807 1096-620X. 10.1089/jmf.2017.0086 |
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 |
Mary Ann Liebert |
publisher.none.fl_str_mv |
Mary Ann Liebert |
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 |
|
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1799133463194894336 |