Effect of Chlorogenic Acid (5-Caffeoylquinic Acid) Isolated from Baccharis oxyodonta on the Structure and Pharmacological Activities of Secretory Phospholipase A2 from Crotalus durissus terrificus
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1155/2014/726585 http://hdl.handle.net/11449/117238 |
Resumo: | The aim of this paper was to investigate the effect of chlorogenic acid (5-caffeoylquinic acid, 5CQA), isolated from Baccharis oxyodonta, on the structure and pharmacological effect of secretory phospholipase A2 (sPLA2) from Crotalus durissus terrificus. All in vitro and in vivo experiments were conducted using a purified sPLA2 compared under the same experimental conditions with sPLA2 : 5CQA. 5CQA induced several discrete modifications in the secondary structure and the hydrophobic characteristics of native sPLA2 that induced slight changes in the alpha-helical content, increase in the randomcoil structure, and decrease of fluorescence of native sPLA2. Moreover, 5CQA significantly decreased the enzymatic activity and the oedema and myonecrosis induced by native sPLA2. As the catalytic activity of sPLA2 plays an important role in several of its biological and pharmacological properties, antibacterial activity was used to confirm the decrease in its enzymatic activity by 5CQA, which induced massive bacterial cell destruction. We found that 5CQA specifically abolished the enzymatic activity of sPLA2 and induced discrete protein unfolding that mainly involved the pharmacological site of sPLA2. These results showed the potential application of 5CQA in the snake poisoning treatment and modulation of the pathological effect of inflammation induced by secretory PLA2. |
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Effect of Chlorogenic Acid (5-Caffeoylquinic Acid) Isolated from Baccharis oxyodonta on the Structure and Pharmacological Activities of Secretory Phospholipase A2 from Crotalus durissus terrificusThe aim of this paper was to investigate the effect of chlorogenic acid (5-caffeoylquinic acid, 5CQA), isolated from Baccharis oxyodonta, on the structure and pharmacological effect of secretory phospholipase A2 (sPLA2) from Crotalus durissus terrificus. All in vitro and in vivo experiments were conducted using a purified sPLA2 compared under the same experimental conditions with sPLA2 : 5CQA. 5CQA induced several discrete modifications in the secondary structure and the hydrophobic characteristics of native sPLA2 that induced slight changes in the alpha-helical content, increase in the randomcoil structure, and decrease of fluorescence of native sPLA2. Moreover, 5CQA significantly decreased the enzymatic activity and the oedema and myonecrosis induced by native sPLA2. As the catalytic activity of sPLA2 plays an important role in several of its biological and pharmacological properties, antibacterial activity was used to confirm the decrease in its enzymatic activity by 5CQA, which induced massive bacterial cell destruction. We found that 5CQA specifically abolished the enzymatic activity of sPLA2 and induced discrete protein unfolding that mainly involved the pharmacological site of sPLA2. These results showed the potential application of 5CQA in the snake poisoning treatment and modulation of the pathological effect of inflammation induced by secretory PLA2.Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Fundo Mackenzie de PesquisaConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)UNESP, BR-11330900 Sao Vicente, SP, BrazilUniv Sao Paulo, Inst Biociencias, Dept Bot, BR-05508090 Sao Paulo, BrazilUniv Presbiteriana Mackenzie, Escola Engn, Curso Quim, BR-01302907 Sao Paulo, BrazilUniv Presbiteriana Mackenzie, Ctr Ciencias Biol & Saude, Curso Ciencias Biol, BR-01302907 Sao Paulo, BrazilUNESP, BR-11330900 Sao Vicente, SP, BrazilFAPESP: 11/06704-4Hindawi Publishing CorporationUniversidade Estadual Paulista (Unesp)Universidade de São Paulo (USP)Univ Presbiteriana MackenzieToyama, Daniela O. [UNESP]Ferreira, Marcelo J. P.Romoff, PauleteFavero, Oriana A.Gaeta, Henrique H. [UNESP]Toyama, Marcos H. [UNESP]2015-03-18T15:55:37Z2015-03-18T15:55:37Z2014-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article10application/epub+zipapplication/pdfhttp://dx.doi.org/10.1155/2014/726585Biomed Research International. New York: Hindawi Publishing Corporation, 10 p., 2014.2314-6133http://hdl.handle.net/11449/11723810.1155/2014/726585WOS:000345403500001WOS000345403500001.pdfWOS000345403500001.epubWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBiomed Research International2.5830,935info:eu-repo/semantics/openAccess2023-12-22T06:21:53Zoai:repositorio.unesp.br:11449/117238Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-12-22T06:21:53Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Effect of Chlorogenic Acid (5-Caffeoylquinic Acid) Isolated from Baccharis oxyodonta on the Structure and Pharmacological Activities of Secretory Phospholipase A2 from Crotalus durissus terrificus |
title |
Effect of Chlorogenic Acid (5-Caffeoylquinic Acid) Isolated from Baccharis oxyodonta on the Structure and Pharmacological Activities of Secretory Phospholipase A2 from Crotalus durissus terrificus |
spellingShingle |
Effect of Chlorogenic Acid (5-Caffeoylquinic Acid) Isolated from Baccharis oxyodonta on the Structure and Pharmacological Activities of Secretory Phospholipase A2 from Crotalus durissus terrificus Toyama, Daniela O. [UNESP] |
title_short |
Effect of Chlorogenic Acid (5-Caffeoylquinic Acid) Isolated from Baccharis oxyodonta on the Structure and Pharmacological Activities of Secretory Phospholipase A2 from Crotalus durissus terrificus |
title_full |
Effect of Chlorogenic Acid (5-Caffeoylquinic Acid) Isolated from Baccharis oxyodonta on the Structure and Pharmacological Activities of Secretory Phospholipase A2 from Crotalus durissus terrificus |
title_fullStr |
Effect of Chlorogenic Acid (5-Caffeoylquinic Acid) Isolated from Baccharis oxyodonta on the Structure and Pharmacological Activities of Secretory Phospholipase A2 from Crotalus durissus terrificus |
title_full_unstemmed |
Effect of Chlorogenic Acid (5-Caffeoylquinic Acid) Isolated from Baccharis oxyodonta on the Structure and Pharmacological Activities of Secretory Phospholipase A2 from Crotalus durissus terrificus |
title_sort |
Effect of Chlorogenic Acid (5-Caffeoylquinic Acid) Isolated from Baccharis oxyodonta on the Structure and Pharmacological Activities of Secretory Phospholipase A2 from Crotalus durissus terrificus |
author |
Toyama, Daniela O. [UNESP] |
author_facet |
Toyama, Daniela O. [UNESP] Ferreira, Marcelo J. P. Romoff, Paulete Favero, Oriana A. Gaeta, Henrique H. [UNESP] Toyama, Marcos H. [UNESP] |
author_role |
author |
author2 |
Ferreira, Marcelo J. P. Romoff, Paulete Favero, Oriana A. Gaeta, Henrique H. [UNESP] Toyama, Marcos H. [UNESP] |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Universidade de São Paulo (USP) Univ Presbiteriana Mackenzie |
dc.contributor.author.fl_str_mv |
Toyama, Daniela O. [UNESP] Ferreira, Marcelo J. P. Romoff, Paulete Favero, Oriana A. Gaeta, Henrique H. [UNESP] Toyama, Marcos H. [UNESP] |
description |
The aim of this paper was to investigate the effect of chlorogenic acid (5-caffeoylquinic acid, 5CQA), isolated from Baccharis oxyodonta, on the structure and pharmacological effect of secretory phospholipase A2 (sPLA2) from Crotalus durissus terrificus. All in vitro and in vivo experiments were conducted using a purified sPLA2 compared under the same experimental conditions with sPLA2 : 5CQA. 5CQA induced several discrete modifications in the secondary structure and the hydrophobic characteristics of native sPLA2 that induced slight changes in the alpha-helical content, increase in the randomcoil structure, and decrease of fluorescence of native sPLA2. Moreover, 5CQA significantly decreased the enzymatic activity and the oedema and myonecrosis induced by native sPLA2. As the catalytic activity of sPLA2 plays an important role in several of its biological and pharmacological properties, antibacterial activity was used to confirm the decrease in its enzymatic activity by 5CQA, which induced massive bacterial cell destruction. We found that 5CQA specifically abolished the enzymatic activity of sPLA2 and induced discrete protein unfolding that mainly involved the pharmacological site of sPLA2. These results showed the potential application of 5CQA in the snake poisoning treatment and modulation of the pathological effect of inflammation induced by secretory PLA2. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-01-01 2015-03-18T15:55:37Z 2015-03-18T15:55:37Z |
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://dx.doi.org/10.1155/2014/726585 Biomed Research International. New York: Hindawi Publishing Corporation, 10 p., 2014. 2314-6133 http://hdl.handle.net/11449/117238 10.1155/2014/726585 WOS:000345403500001 WOS000345403500001.pdf WOS000345403500001.epub |
url |
http://dx.doi.org/10.1155/2014/726585 http://hdl.handle.net/11449/117238 |
identifier_str_mv |
Biomed Research International. New York: Hindawi Publishing Corporation, 10 p., 2014. 2314-6133 10.1155/2014/726585 WOS:000345403500001 WOS000345403500001.pdf WOS000345403500001.epub |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Biomed Research International 2.583 0,935 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
10 application/epub+zip application/pdf |
dc.publisher.none.fl_str_mv |
Hindawi Publishing Corporation |
publisher.none.fl_str_mv |
Hindawi Publishing Corporation |
dc.source.none.fl_str_mv |
Web of Science reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
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1803650053523374080 |