title: Neutralization of pharmacological and toxic activities of bothrops snake venoms by Schizolobium parahyba (Fabaceae) aqueous extract and its fractions.
abstract: The aqueous extract prepared from Schizolobium parahyba (Sp) leaves, a native plant from Atlantic Forest (Brazil), was tested to analyse its ability to inhibit some biological and enzymatic activities induced by Bothrops alternatus (BaltCV) and Bothrops moojeni (BmooCV) snake venoms. Sp inhibited 100% of lethality, blood incoagulability, haemorrhagic and indirect haemolytic activities at a 1:10 ratio (venom/extract, w/w), as well as coagulant activity at a 1:5 ratio (venom/extract, w/w) induced by both venoms. BaltCV fibrinogenolytic activity was also neutralized by Sp at a 1:10 ratio, resulting in total protection of fibrinogen Bbeta chain and partial protection of Aalpha chain. Interaction tests have demonstrated that, at certain extract/proteins ratios, Sp precipitates proteins non-specifically suggesting the presence of tannins, which are very likely responsible for the excellent inhibiting effects of the analysed ophidian activities. Sp aqueous extract chromatography on Sephadex LH-20 was carried out aiming at the separation of these compounds that mask the obtained results. Thus, the fractionation of Sp resulted in three fractions: F1 (methanolic fraction); F2 (methanol:water fraction, 1:1 v/v); and F3 (aqueous fraction). These fractions were analysed for their ability to inhibit the BaltCV fibrinogenolytic activity. F1 inhibited 100% the venom fibrinogenolytic activity without presenting protein precipitation effect; F2 showed only partial inhibition of this venom activity. Finally, F3 did not inhibit fibrinogen proteolysis, but presented strong protein precipitating action. We conclude that Sp aqueous extract, together with tannins, also contains other compounds that can display specific inhibitory activity against snake venom toxins.
authors.affiliation: Institute of Genetic and Biochemical, University of Uberlândia, UFU, Uberlândia/MG, Brazil.
authors.forename: Luis Henrique F
authors.initials: LH
authors.lastname: Vale
authors.forename: Mirian M
authors.initials: MM
authors.lastname: Mendes
authors.forename: Amélia
authors.initials: A
authors.lastname: Hamaguchi
authors.forename: Andreimar M
authors.initials: AM
authors.lastname: Soares
authors.forename: Veridiana M
authors.initials: VM
authors.lastname: Rodrigues
authors.forename: Maria Inês
authors.initials: MI
authors.lastname: Homsi-Brandeburgo
mesh_terms: D000818:Animals; D000925:Anticoagulants / Q000737:chemistry / Q000494:pharmacology*; D000933:Antifibrinolytic Agents / Q000737:chemistry / Q000494:pharmacology*; D001777:Blood Coagulation / Q000187:drug effects; D017837:Bothrops; D002850:Chromatography, Gel; D007887:Fabaceae / Q000737:chemistry*; D005340:Fibrinogen / Q000378:metabolism; D006470:Hemorrhage / Q000517:prevention & control; D008297:Male; D051379:Mice; D064801:Phospholipase A2 Inhibitors; D054467:Phospholipases A2 / Q000378:metabolism; D010936:Plant Extracts / Q000737:chemistry / Q000494:pharmacology; D018515:Plant Leaves / Q000737:chemistry; D013634:Tannins / Q000737:chemistry / Q000494:pharmacology; D014757:Viper Venoms / Q000037:antagonists & inhibitors / Q000201:enzymology / Q000633:toxicity*
chemical_list: D000925:Anticoagulants; D000933:Antifibrinolytic Agents; D064801:Phospholipase A2 Inhibitors; D010936:Plant Extracts; D013634:Tannins; D014757:Viper Venoms; D005340:Fibrinogen; D054467:Phospholipases A2