The inhibitory potential of the condensed-tannin-rich fraction of Plathymenia reticulata Benth. (Fabaceae) against Bothrops atrox envenomation

Moura, Valéria Mourão de; Silva, Wânia Cristina Rodrigues da; Raposo, Juliana Divina Almeida; Freitas-de-Sousa, Luciana Aparecida; Dos-Santos, Maria Cristina; Oliveira, Rodrigo Santos de; Mourão, Rosa Helena Veras

doi:10.1016/j.jep.2016.02.047

Cited by 28 publications

(27 citation statements)

References 25 publications

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“…According to Moura et al [16] the formation of complexes between plant compounds and calcium ions can interfere in their (Ca 2 + ) binding to phospholipases A 2 , and consequently affecting the performance of their function as cofactors. In the present work, however, the evaluated extracts of L. sidoides did not show activity as inhibitors of phospholipases.…”

Section: Resultsmentioning

confidence: 99%

Prospection of Enzyme Modulators in Aqueous and Ethanolic Extracts of Lippia sidoides Leaves: Genotoxicity, Digestion, Inflammation, and Hemostasis

Braga

Abreu

Trento

et al. 2019

Chemistry & Biodiversity

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The aqueous and ethanolic extracts of Lippia sidoides Cham. were chemically characterized and tested for their action on enzymes involved in processes such as inflammation, blood coagulation, and digestion. Both extracts potentiated the activity of phospholipases A2 present in the venom of Bothrops atrox in 12 % and completely inhibited the hemolysis induced by B. jararacussu and B. moojeni venoms in the proportions between 1 : 0.5 and 1 : 5 (venom/extracts (w/w)). They inhibited the thrombolysis induced by B. moojeni (10 to 25 %), potentiated the thrombolysis induced by the Lachesis muta muta venom (30 to 80 %), prolonged the coagulation time induced by B. moojeni and L. muta muta venoms, and presented antigenotoxic action. Both extracts reduced the activity of α‐glycosidases, the aqueous extract inhibited lipases, and the ethanolic extract inhibited α‐amylases. The results demonstrate the modulatory action of the extracts on proteases, phospholipases, and digestive enzymes. In addition, the rich phenolic composition of these extracts highlights their potential for nutraceutical use.

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Section: Resultsmentioning

confidence: 99%

Prospection of Enzyme Modulators in Aqueous and Ethanolic Extracts of Lippia sidoides Leaves: Genotoxicity, Digestion, Inflammation, and Hemostasis

Braga

Abreu

Trento

et al. 2019

Chemistry & Biodiversity

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“…These compounds can also form complexes with divalent ions such as calcium, an essential cofactor for phospholipases A 2 and other enzymes involved in the coagulation cascade. This chelating action is responsible for impairing the action of phospholipases A 2 (Moura et al., ; Pithayanukul et al., ). Catechin and epicatechin, identified on both extracts, were reported to interfere with the catalytic site of snake toxins, decreasing its activity (Santhosh et al., ).…”

Section: Resultsmentioning

confidence: 99%

Fruit Bagasse Phytochemicals from Malpighia Emarginata Rich in Enzymatic Inhibitor with Modulatory Action on Hemostatic Processes

Marques

César

Braga

et al. 2018

Journal of Food Science

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Agro‐industrial wastes are promising sources of phytochemicals for the development of products to be used in health promotion and maintenance. In this study, extracts from acerola bagasse (AB) were characterized by HPLC, and evaluated according to its modulatory action on phospholipases A2 and proteases involved in processes such as inflammation and blood clotting. Snake venoms were used as biological tools once they have high functional and structural homology between their enzymes and human enzymes. Two types of extracts were prepared from AB: aqueous and methanolic. These extracts, evaluated at different proportions (venom:extract, w:w), significantly inhibited the phospholipase activity induced by the venoms of Bothrops moojeni, Bothrops atrox (11% to 31%), and Crotalus durissus terrificus (C. d. t.) (11% to 19%). The hemolytic activity induced by the venoms of B. moojeni and C. d. t. was better inhibited by the methanolic extract (inhibition between 23% and 48%). Thrombolysis induced by the venoms of B. moojeni and C. d. t. was inhibited by both extracts, with inhibition ranging from 13% to 63% for the aqueous extract, and from 12% to 92% for the methanolic one. Both extracts increased the time of coagulation induced by the venoms of B. moojeni and Lachesis muta muta in 26 and up to 68 s. These inhibitory actions were related to the following phenolic compounds present in the extract of AB: gallic acid, catechin, epigallocatechin gallate, epicatechin, syringic acid, p‐coumaric acid, and quercetin. Additional studies are needed to confirm their potential use for nutraceutical purposes. Practical Application Agro‐industrial wastes are promising sources of phytochemicals for the development of products that can be used by pharmaceutical, cosmetics, and food industries. Studies report the use of the acerola bagasse extract in health improvement. However, its toxic‐pharmacological characterization is still scarce. In this study, the extracts of acerola bagasse presented phenolic compounds that can modulate the activity of enzymes such as phospholipases A2 and proteases that act on the coagulant/anticoagulant and thrombotic/thrombolytic activities and the break of phospholipids, decreasing the inflammation and platelet aggregation. Although the in vivo effects of the extracts are not fully understood, this study shed light upon the possibilities of their usage.

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“…Some mechanisms of action have been proposed for several phenolic compounds. The sequestration of metal ions, which are enzymatic cofactors, suits as an example . Pithayanukul et al, observed partial inhibition of the enzymatic activity of metalloproteases present in the venoms of Calloselasma rhodostoma and Naja naja kaouthia .…”

Section: Discussionmentioning

confidence: 99%

“…According to Cotrim et al, 25 the flavonoid quercetin was able to inhibit 40% of the phospholipase activity induced by the venom of C. durissus terrificus, due to its ability to bind to the amide groups of different proteins by strong hydrogen bonds. 26 Moura et al 23 reported that tannins can form complexes with calcium, which is a cofactor of PLA 2 and several enzymes involved in the coagulation cascade.…”

Section: Discussionmentioning

confidence: 99%

Molecular interactions between p‐coumaric acid and snake venom toxins

César

Trento

Sales

et al. 2019

J of Cellular Biochemistry

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A large number of natural compounds, such as phenolic compounds, have been scientifically evaluated in the search for enzyme inhibitors. The interactions between the phenolic compound p‐coumaric acid and the enzymes present in snake venoms (used as research tools) were evaluated in vitro and in silico. The p‐coumaric acid was able to inhibit 31% of the phospholipase activity induced by Bothrops alternatus venom, 27% of the hemolytic activity induced by B. moojeni, 62.5% of the thrombolytic activity induced by B. jararacussu, and approximately 27% of the activity thrombosis induced by Crotalus durissus terrificus. Previous incubation of p‐coumaric acid with the venoms of B. atrox and B. jararacussu increased the coagulation time by 2.18 and 2.16‐fold, respectively. The activity of serine proteases in B. atrox and B. jararacussu venoms was reduced by 60% and 66.34%, respectively. Computational chemistry analyses suggests the specific binding of p‐coumaric acid to the active site of proteases through hydrogen and hydrophobic interactions. The phenolic compound evaluated in this work has great potential in therapeutic use to both prevent and treat hemostatic alterations, because the venom proteins inhibited by the p‐coumaric acid have high homology with human proteins that have a fundamental role in several pathologies.

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The inhibitory potential of the condensed-tannin-rich fraction of Plathymenia reticulata Benth. (Fabaceae) against Bothrops atrox envenomation

Abstract: Our findings indicate that CTPr could be a good source of natural inhibitors of the components of snake venom responsible for inducing local inflammation.

Cited by 28 publications

References 25 publications

Prospection of Enzyme Modulators in Aqueous and Ethanolic Extracts of Lippia sidoides Leaves: Genotoxicity, Digestion, Inflammation, and Hemostasis

Prospection of Enzyme Modulators in Aqueous and Ethanolic Extracts of Lippia sidoides Leaves: Genotoxicity, Digestion, Inflammation, and Hemostasis

Fruit Bagasse Phytochemicals from Malpighia Emarginata Rich in Enzymatic Inhibitor with Modulatory Action on Hemostatic Processes

Molecular interactions between p‐coumaric acid and snake venom toxins

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