Vanillic acid as phospholipase A 2 and proteases inhibitor: In vitro and computational analyses

• Published in: Biotechnology and applied biochemistry 2020-05
• Main Authors: Cesar, Pedro H S, Trento, Marcus V, Sales, Thais A, Simão, Anderson A, Ramalho, Teodorico C, Marcussi, Silvana
• Format: Article
• Language: English
• ISSN: 1470-8744

Enzymatic inhibition by natural compounds may represent a valuable adjuvant in snakebite serum therapy.The objective in this work was to evaluate possible in vitro interactions between vanillic acid and enzymes from Bothrops spp. and Crotalus durissus terrificus venoms, and also suggest a theory as how they interact based on molecular docking. Vanillic acid inhibited the phospholipase activity induced by B. alternatus (∼25% inhibition), the caseinolytic activity induced by B. atrox (∼30%), B. jararacussu (∼44%), and C. d. terrificus (∼33%), the fibrinogenolysis induced by B. jararacussu, B. atrox, and C. d. terrificus (100%), the serine protease activity induced by B. moojeni (∼45%) and B. jararaca (∼66%), the hemolytic activity induced by B. moojeni (∼26%), the thrombolysis activity induced by B. atrox (∼30%) and B. jararacussu (∼20%), and the thrombotic activity induced by C. d. terrificus (∼8%). The compound was also capable of delaying the coagulation time in citrated plasma by 60, 35, and 75 seconds, when incubated with B. moojeni, B. atrox, and B. jararaca, respectively. The results obtained expand the possibilities for future pharmaceutical use of vanillic acid, considering the high homology degree among human and snake venom phospholipases A and proteases (involved in chronic inflammatory diseases). Also, this compound can be used as adjuvant to improve currently available treatments for ophidism victims. This article is protected by copyright. All rights reserved.