Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (<i>Laguncularia racemosa</i>) Leaves, on Snake Venom Secretory Phospholipase A2
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 is...
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| Format: | Article |
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MDPI AG
2019-07-01
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| Series: | Marine Drugs |
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| Online Access: | https://www.mdpi.com/1660-3397/17/7/403 |
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| author | Caroline Fabri Bittencourt Rodrigues Marcelo José Pena Ferreira Mariana Novo Belchor Caroline R. C. Costa Danielle P. Novaes Adeilso Bispo dos Santos Junior Cinthia I. Tamayose Marcus Vinícius Terashima Pinho Marcos Antonio de Oliveira Marcos Hikari Toyama |
| author_facet | Caroline Fabri Bittencourt Rodrigues Marcelo José Pena Ferreira Mariana Novo Belchor Caroline R. C. Costa Danielle P. Novaes Adeilso Bispo dos Santos Junior Cinthia I. Tamayose Marcus Vinícius Terashima Pinho Marcos Antonio de Oliveira Marcos Hikari Toyama |
| author_sort | Caroline Fabri Bittencourt Rodrigues |
| collection | DOAJ |
| 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 <i>Laguncularia racemosa</i> leaves. The pharmacological and biological effects of Casu were evaluated on isolated sPLA2 from the rattlesnake (<i>Crotalus durissus terrificus</i>) 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. |
| first_indexed | 2024-04-11T10:59:44Z |
| format | Article |
| id | doaj.art-8d0beed37231446d85b388cd99afea11 |
| institution | Directory Open Access Journal |
| issn | 1660-3397 |
| language | English |
| last_indexed | 2024-04-11T10:59:44Z |
| publishDate | 2019-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Marine Drugs |
| spelling | doaj.art-8d0beed37231446d85b388cd99afea112022-12-22T04:28:38ZengMDPI AGMarine Drugs1660-33972019-07-0117740310.3390/md17070403md17070403Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (<i>Laguncularia racemosa</i>) Leaves, on Snake Venom Secretory Phospholipase A2Caroline Fabri Bittencourt Rodrigues0Marcelo José Pena Ferreira1Mariana Novo Belchor2Caroline R. C. Costa3Danielle P. Novaes4Adeilso Bispo dos Santos Junior5Cinthia I. Tamayose6Marcus Vinícius Terashima Pinho7Marcos Antonio de Oliveira8Marcos Hikari Toyama9Laboratório de Bioquímica e Biologia Molecular de Peptídeos (BIOMOLPEP), Instituto de Biociências, UNESP, Campus do Litoral Paulista, São Vicente 11330-900, São Paulo, BrazilDepartamento de Botânica, Instituto de Biociências, Universidade de São Paulo, São Paulo 05508-090, BrazilLaboratório de Bioquímica e Biologia Molecular de Peptídeos (BIOMOLPEP), Instituto de Biociências, UNESP, Campus do Litoral Paulista, São Vicente 11330-900, São Paulo, BrazilLaboratório de Bioquímica e Biologia Molecular de Peptídeos (BIOMOLPEP), Instituto de Biociências, UNESP, Campus do Litoral Paulista, São Vicente 11330-900, São Paulo, BrazilLaboratório de Bioquímica e Biologia Molecular de Peptídeos (BIOMOLPEP), Instituto de Biociências, UNESP, Campus do Litoral Paulista, São Vicente 11330-900, São Paulo, BrazilLaboratório de Bioquímica e Biologia Molecular de Peptídeos (BIOMOLPEP), Instituto de Biociências, UNESP, Campus do Litoral Paulista, São Vicente 11330-900, São Paulo, BrazilDepartamento de Botânica, Instituto de Biociências, Universidade de São Paulo, São Paulo 05508-090, BrazilLaboratório de Bioquímica e Biologia Molecular de Peptídeos (BIOMOLPEP), Instituto de Biociências, UNESP, Campus do Litoral Paulista, São Vicente 11330-900, São Paulo, BrazilLaboratório de Biologia Molecular Estrutural (LABIMES), Instituto de Biociências, UNESP, Campus do Litoral Paulista, São Vicente 11330-900, São Paulo, BrazilLaboratório de Bioquímica e Biologia Molecular de Peptídeos (BIOMOLPEP), Instituto de Biociências, UNESP, Campus do Litoral Paulista, São Vicente 11330-900, São Paulo, BrazilEllagitannins 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 <i>Laguncularia racemosa</i> leaves. The pharmacological and biological effects of Casu were evaluated on isolated sPLA2 from the rattlesnake (<i>Crotalus durissus terrificus</i>) 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.https://www.mdpi.com/1660-3397/17/7/403casuarictin<i>Laguncularia racemosa</i>secretory phospholipase A2<i>Crotalus durissus terrificus</i>enzymatic inhibitionanti-inflammatoryedema and myonecrosis |
| spellingShingle | Caroline Fabri Bittencourt Rodrigues Marcelo José Pena Ferreira Mariana Novo Belchor Caroline R. C. Costa Danielle P. Novaes Adeilso Bispo dos Santos Junior Cinthia I. Tamayose Marcus Vinícius Terashima Pinho Marcos Antonio de Oliveira Marcos Hikari Toyama Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (<i>Laguncularia racemosa</i>) Leaves, on Snake Venom Secretory Phospholipase A2 Marine Drugs casuarictin <i>Laguncularia racemosa</i> secretory phospholipase A2 <i>Crotalus durissus terrificus</i> enzymatic inhibition anti-inflammatory edema and myonecrosis |
| title | Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (<i>Laguncularia racemosa</i>) Leaves, on Snake Venom Secretory Phospholipase A2 |
| title_full | Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (<i>Laguncularia racemosa</i>) Leaves, on Snake Venom Secretory Phospholipase A2 |
| title_fullStr | Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (<i>Laguncularia racemosa</i>) Leaves, on Snake Venom Secretory Phospholipase A2 |
| title_full_unstemmed | Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (<i>Laguncularia racemosa</i>) Leaves, on Snake Venom Secretory Phospholipase A2 |
| title_short | Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (<i>Laguncularia racemosa</i>) Leaves, on Snake Venom Secretory Phospholipase A2 |
| title_sort | evaluation of the inhibitory potential of casuarictin an ellagitannin isolated from white mangrove i laguncularia racemosa i leaves on snake venom secretory phospholipase a2 |
| topic | casuarictin <i>Laguncularia racemosa</i> secretory phospholipase A2 <i>Crotalus durissus terrificus</i> enzymatic inhibition anti-inflammatory edema and myonecrosis |
| url | https://www.mdpi.com/1660-3397/17/7/403 |
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