scholarly journals Evaluation of the Inhibitory Potential of Casuarictin, an Ellagitannin Isolated from White Mangrove (Laguncularia racemosa) Leaves, on Snake Venom Secretory Phospholipase A2

Marine Drugs ◽  
2019 ◽  
Vol 17 (7) ◽  
pp. 403 ◽  
Author(s):  
Caroline Fabri Bittencourt Rodrigues ◽  
Marcelo José Pena Ferreira ◽  
Mariana Novo Belchor ◽  
Caroline R. C. Costa ◽  
Danielle P. Novaes ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Biological Effects ◽  
Laguncularia Racemosa ◽  
Laser Desorption Ionization ◽  
Secretory Phospholipase A2 ◽  
Ionization Time ◽  
Secretory Phospholipase ◽  
Flight Mass Spectrometry ◽  
Inhibitory Potential ◽  
Crotalus Durissus

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.

Evaluation of a hydrolysable tannin purified from Laguncularia racemosa leaves against edema and myonecrosis induced by secretory phospholipase A2 isolated from Crotalus durissus terrificus venom

Toxicon ◽  
2020 ◽  
Vol 177 ◽  
pp. S48-S49
Author(s):  
Caroline Fabri Bittencourt Rodrigues ◽  
Marcelo José Pena Ferreira ◽  
Mariana Novo Belchor ◽  
Caroline R.C. Costa ◽  
Danielle P. Novaes ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Laguncularia Racemosa ◽  
Secretory Phospholipase A2 ◽  
Hydrolysable Tannin ◽  
Crotalus Durissus Terrificus ◽  
Secretory Phospholipase ◽  
Crotalus Durissus

Fast and efficient procedure for purification of secretory phospholipase A2 (SPLA2) from Crotalus durissus terrificus venom using a solid phase extraction

Toxicon ◽  
2020 ◽  
Vol 177 ◽  
pp. S49
Author(s):  
Airam Roggero dos Santos Silva ◽  
Laila Lucyane Ferreira de Moraes ◽  
Mariana Novo Belchor ◽  
Caroline R.C. Costa ◽  
Danielle P. Novaes ◽  
...  
Keyword(s):  
Solid Phase Extraction ◽  
Phospholipase A2 ◽  
Solid Phase ◽  
Phase Extraction ◽  
Secretory Phospholipase A2 ◽  
Efficient Procedure ◽  
Crotalus Durissus Terrificus ◽  
Secretory Phospholipase ◽  
Crotalus Durissus

scholarly journals Modulation of the Pharmacological Activities of Secretory Phospholipase A2 from Crotalus durissus cascavella Induced by Naringin

Molecules ◽  
2011 ◽  
Vol 16 (1) ◽  
pp. 738-761 ◽  
Author(s):  
Marcelo L. Santos ◽  
Daniela O. Toyama ◽  
Simone C. B. Oliveira ◽  
Camila A. Cotrim ◽  
Eduardo B. S. Diz-Filho ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Secretory Phospholipase A2 ◽  
Pharmacological Activities ◽  
Secretory Phospholipase ◽  
Crotalus Durissus Cascavella ◽  
Crotalus Durissus

scholarly journals Bioaffinity Fishing Procedure Using Secretory Phospholipase A2 for Screening for Bioactive Components: Modulation of Pharmacological Effect Induced by sPLA2 from Crotalus durissus terrificus by Hispidulin from Moquiniastrum floribundum

Molecules ◽  
2020 ◽  
Vol 25 (2) ◽  
pp. 282 ◽  
Author(s):  
Adeilso Bispo dos Santos Junior ◽  
Cinthia I. Tamayose ◽  
Marcelo J. P. Ferreira ◽  
Mariana N. Belchor ◽  
Caroline R. C. Costa ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
High Selectivity ◽  
Secretory Phospholipase A2 ◽  
Bioactive Components ◽  
Crotalus Durissus Terrificus ◽  
Secretory Phospholipase ◽  
Spla2 Activity ◽  
Screening And Identification ◽  
Isolated Compound ◽  
Crotalus Durissus

Bioaffinity capturing of molecules allows the discovery of bioactive compounds and decreases the need for various stages in the natural compound isolation process. Despite the high selectivity of this technique, the screening and identification methodology depends on the presence of a protein to capture potential ligands. However, some proteins, such as snake secretory phospholipase A2 (sPLA2), have never been investigated using this approach. The purpose of this study was to evaluate the use of a new method for screening natural compounds using a bioaffinity-guided ultrafiltration method on Crotalus durissus terrificus sPLA2 followed by HPLC-MS to identify the compounds, and this method could be used to discover new anti-inflammatory compounds from the various organisms originating from biodiversity. Different extracts were selected to evaluate their ability to inhibit sPLA2 activity. The extracts were incubated with sPLA2 and the resulting mixture was ultrafiltrated to elute unbound components. The resulting compounds were identified by HPLC-MS. We identified hispidulin as one of the components present in the Moquiniastrum floribundum leaf and evaluated the ability of this isolated compound to neutralize the inflammatory activity of sPLA2 from Crotalus durissus terrificus.

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