Please use this identifier to cite or link to this item: http://repositorio.ufla.br/jspui/handle/1/40922
metadata.artigo.dc.title: Molecular interactions between p‐coumaric acid and snake venom toxins
metadata.artigo.dc.creator: Cesar, Pedro H. S.
Trento, Marcus Vinícius Cardoso
Sales, Thais A.
Marques, Tamara R.
Braga, Mariana A.
Ramalho, Teodorico C.
Marcussi, Silvana
metadata.artigo.dc.subject: Enzyme inhibitors
Phenolic compound
Phospholipases A2
Proteases
metadata.artigo.dc.publisher: Wiley
metadata.artigo.dc.date.issued: Sep-2019
metadata.artigo.dc.identifier.citation: CÉSAR, P. H. S. et al. Molecular interactions between p‐coumaric acid and snake venom toxins. Journal of Cellular Biochemistry, [S.l.], v. 120, n. 9, p. 14594-14603, Sept. 2019.
metadata.artigo.dc.description.abstract: 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.
metadata.artigo.dc.identifier.uri: https://onlinelibrary.wiley.com/doi/abs/10.1002/jcb.28721
http://repositorio.ufla.br/jspui/handle/1/40922
metadata.artigo.dc.language: en_US
Appears in Collections:DQI - Artigos publicados em periódicos

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.