Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.3390/md17070403 http://hdl.handle.net/11449/189380 |
Resumo: | Ellagitannins constitute the largest group of hydrolyzable tannins of plants, and, from this group, casuarictin (Casu) was identified in some plant species. However, to our knowledge, no investigation of secretory phospholipase A2 (sPLA2) inhibition by Casu has been performed yet. Casuarictin was isolated by chromatography n-butanol (n-BuOH) partition of Laguncularia racemosa leaves. The pharmacological and biological effects of Casu were evaluated on isolated sPLA2 from the rattlesnake (Crotalus durissus terrificus) and using a plant bacterial strain. The compound was able to form a protein complex consisting of a stable sPLA2 + Casu complex. Analyses carried out with matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF) revealed that the molecular mass of sPLA2 increased from 14,425.62 to 15,362.74 Da. The enzymatic activity of the sPLA2 + Casu complex was significantly lower than that of native sPLA2. Besides, molecular interactions of Casu with sPLA2 were able to virtually abolish the native edematogenic effect as well as myonecrosis induced by the protein when injected 10 min after sPLA2. Therefore, Casu may be considered a potential anti-inflammatory that can be used to treat edema and myonecrosis induced by serine-secreting phospholipase A2. In addition, the compound also showed great antimicrobial potential. |
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Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2Anti-inflammatoryCasuarictinCrotalus durissus terrificusEdemaEnzymatic inhibitionLaguncularia racemosaMyonecrosisSecretory phospholipase A2Ellagitannins constitute the largest group of hydrolyzable tannins of plants, and, from this group, casuarictin (Casu) was identified in some plant species. However, to our knowledge, no investigation of secretory phospholipase A2 (sPLA2) inhibition by Casu has been performed yet. Casuarictin was isolated by chromatography n-butanol (n-BuOH) partition of Laguncularia racemosa leaves. The pharmacological and biological effects of Casu were evaluated on isolated sPLA2 from the rattlesnake (Crotalus durissus terrificus) and using a plant bacterial strain. The compound was able to form a protein complex consisting of a stable sPLA2 + Casu complex. Analyses carried out with matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF) revealed that the molecular mass of sPLA2 increased from 14,425.62 to 15,362.74 Da. The enzymatic activity of the sPLA2 + Casu complex was significantly lower than that of native sPLA2. Besides, molecular interactions of Casu with sPLA2 were able to virtually abolish the native edematogenic effect as well as myonecrosis induced by the protein when injected 10 min after sPLA2. Therefore, Casu may be considered a potential anti-inflammatory that can be used to treat edema and myonecrosis induced by serine-secreting phospholipase A2. In addition, the compound also showed great antimicrobial potential.National Council for Scientific ResearchUniversidade de São PauloLaboratório de Bioquímica e Biologia Molecular de Peptídeos (BIOMOLPEP) Instituto de Biociências UNESP Campus do Litoral Paulista, São VicenteLaboratório de Herpetologia Instituto Butantan São PauloDepartamento de Botânica Instituto de Biociências Universidade de São PauloLaboratório de Biologia Molecular Estrutural (LABIMES) Instituto de Biociências UNESP Campus do Litoral Paulista, São VicenteLaboratório de Bioquímica e Biologia Molecular de Peptídeos (BIOMOLPEP) Instituto de Biociências UNESP Campus do Litoral Paulista, São VicenteLaboratório de Biologia Molecular Estrutural (LABIMES) Instituto de Biociências UNESP Campus do Litoral Paulista, São VicenteNational Council for Scientific Research: 001Universidade de São Paulo: 2013/10938-6Universidade de São Paulo: 2014/20932-8Universidade de São Paulo: 2014/21593-2Universidade de São Paulo: 2017/20291-0Universidade Estadual Paulista (Unesp)São PauloUniversidade de São Paulo (USP)Rodrigues, Caroline Fabri Bittencourt [UNESP]Ferreira, Marcelo José PenaBelchor, Mariana Novo [UNESP]Costa, Caroline R.C. [UNESP]Novaes, Danielle P. [UNESP]dos Santos, Adeilso Bispo [UNESP]Tamayose, Cinthia I.Pinho, Marcus Vinícius Terashima [UNESP]de Oliveira, Marcos Antonio [UNESP]Toyama, Marcos Hikari [UNESP]2019-10-06T16:38:46Z2019-10-06T16:38:46Z2019-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.3390/md17070403Marine Drugs, v. 17, n. 7, 2019.1660-3397http://hdl.handle.net/11449/18938010.3390/md170704032-s2.0-850685958338573195327542061Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengMarine Drugsinfo:eu-repo/semantics/openAccess2021-10-23T17:30:11Zoai:repositorio.unesp.br:11449/189380Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T15:50:31.995687Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2 |
title |
Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2 |
spellingShingle |
Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2 Rodrigues, Caroline Fabri Bittencourt [UNESP] Anti-inflammatory Casuarictin Crotalus durissus terrificus Edema Enzymatic inhibition Laguncularia racemosa Myonecrosis Secretory phospholipase A2 |
title_short |
Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2 |
title_full |
Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2 |
title_fullStr |
Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2 |
title_full_unstemmed |
Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2 |
title_sort |
Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2 |
author |
Rodrigues, Caroline Fabri Bittencourt [UNESP] |
author_facet |
Rodrigues, Caroline Fabri Bittencourt [UNESP] Ferreira, Marcelo José Pena Belchor, Mariana Novo [UNESP] Costa, Caroline R.C. [UNESP] Novaes, Danielle P. [UNESP] dos Santos, Adeilso Bispo [UNESP] Tamayose, Cinthia I. Pinho, Marcus Vinícius Terashima [UNESP] de Oliveira, Marcos Antonio [UNESP] Toyama, Marcos Hikari [UNESP] |
author_role |
author |
author2 |
Ferreira, Marcelo José Pena Belchor, Mariana Novo [UNESP] Costa, Caroline R.C. [UNESP] Novaes, Danielle P. [UNESP] dos Santos, Adeilso Bispo [UNESP] Tamayose, Cinthia I. Pinho, Marcus Vinícius Terashima [UNESP] de Oliveira, Marcos Antonio [UNESP] Toyama, Marcos Hikari [UNESP] |
author2_role |
author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) São Paulo Universidade de São Paulo (USP) |
dc.contributor.author.fl_str_mv |
Rodrigues, Caroline Fabri Bittencourt [UNESP] Ferreira, Marcelo José Pena Belchor, Mariana Novo [UNESP] Costa, Caroline R.C. [UNESP] Novaes, Danielle P. [UNESP] dos Santos, Adeilso Bispo [UNESP] Tamayose, Cinthia I. Pinho, Marcus Vinícius Terashima [UNESP] de Oliveira, Marcos Antonio [UNESP] Toyama, Marcos Hikari [UNESP] |
dc.subject.por.fl_str_mv |
Anti-inflammatory Casuarictin Crotalus durissus terrificus Edema Enzymatic inhibition Laguncularia racemosa Myonecrosis Secretory phospholipase A2 |
topic |
Anti-inflammatory Casuarictin Crotalus durissus terrificus Edema Enzymatic inhibition Laguncularia racemosa Myonecrosis Secretory phospholipase A2 |
description |
Ellagitannins constitute the largest group of hydrolyzable tannins of plants, and, from this group, casuarictin (Casu) was identified in some plant species. However, to our knowledge, no investigation of secretory phospholipase A2 (sPLA2) inhibition by Casu has been performed yet. Casuarictin was isolated by chromatography n-butanol (n-BuOH) partition of Laguncularia racemosa leaves. The pharmacological and biological effects of Casu were evaluated on isolated sPLA2 from the rattlesnake (Crotalus durissus terrificus) and using a plant bacterial strain. The compound was able to form a protein complex consisting of a stable sPLA2 + Casu complex. Analyses carried out with matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF) revealed that the molecular mass of sPLA2 increased from 14,425.62 to 15,362.74 Da. The enzymatic activity of the sPLA2 + Casu complex was significantly lower than that of native sPLA2. Besides, molecular interactions of Casu with sPLA2 were able to virtually abolish the native edematogenic effect as well as myonecrosis induced by the protein when injected 10 min after sPLA2. Therefore, Casu may be considered a potential anti-inflammatory that can be used to treat edema and myonecrosis induced by serine-secreting phospholipase A2. In addition, the compound also showed great antimicrobial potential. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-10-06T16:38:46Z 2019-10-06T16:38:46Z 2019-01-01 |
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/10.3390/md17070403 Marine Drugs, v. 17, n. 7, 2019. 1660-3397 http://hdl.handle.net/11449/189380 10.3390/md17070403 2-s2.0-85068595833 8573195327542061 |
url |
http://dx.doi.org/10.3390/md17070403 http://hdl.handle.net/11449/189380 |
identifier_str_mv |
Marine Drugs, v. 17, n. 7, 2019. 1660-3397 10.3390/md17070403 2-s2.0-85068595833 8573195327542061 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Marine Drugs |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
Scopus 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 |
|
_version_ |
1808128572743745536 |