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Molecular interactions between p-coumaric acid and snake venom toxins.
Cesar, Pedro H S; Cardoso Trento, Marcus Vinícius; Sales, Thais A; Marques, Tamara R; Braga, Mariana A; Ramalho, Teodorico C; Marcussi, Silvana.
Afiliação
  • Cesar PHS; Biochemistry Laboratory, Departament of Chemistry, Federal University of Lavras, Lavras, Brazil.
  • Cardoso Trento MV; Biochemistry Laboratory, Departament of Chemistry, Federal University of Lavras, Lavras, Brazil.
  • Sales TA; Computational Chemistry Laboratory, Departament of Chemistry, Federal University of Lavras, Lavras, Brazil.
  • Marques TR; Biochemistry Laboratory, Departament of Chemistry, Federal University of Lavras, Lavras, Brazil.
  • Braga MA; Biochemistry Laboratory, Departament of Chemistry, Federal University of Lavras, Lavras, Brazil.
  • Ramalho TC; Computational Chemistry Laboratory, Departament of Chemistry, Federal University of Lavras, Lavras, Brazil.
  • Marcussi S; Biochemistry Laboratory, Departament of Chemistry, Federal University of Lavras, Lavras, Brazil.
J Cell Biochem ; 120(9): 14594-14603, 2019 09.
Article em En | MEDLINE | ID: mdl-31016790
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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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfolipases / Propionatos / Venenos de Serpentes / Serina Proteases / Crotalinae Limite: Animals / Humans Idioma: En Revista: J Cell Biochem Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfolipases / Propionatos / Venenos de Serpentes / Serina Proteases / Crotalinae Limite: Animals / Humans Idioma: En Revista: J Cell Biochem Ano de publicação: 2019 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos