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Molecular interactions between p ‐coumaric acid and snake venom toxins
Author(s) -
Cesar Pedro H. S.,
Cardoso Trento Marcus Vinícius,
Sales Thais A.,
Marques Tamara R.,
Braga Mariana A.,
Ramalho Teodorico C.,
Marcussi Silvana
Publication year - 2019
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.28721
Subject(s) - bothrops , proteases , venom , biochemistry , chemistry , myotoxin , snake venom , enzyme , biology
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.