Abstract
We report here the antiproteolytic and antihemorrhagic properties of triterpenoid saponin inhibitors, named macrolobin-A and B, from Pentaclethra macroloba, against Bothrops snake venoms. The inhibitors were able to neutralize the hemorrhagic, fibrin(ogen)olytic, and proteolytic activities of class P-I and P-III metalloproteases isolated from B. neuwiedi and B. jararacussu venoms. Clotting and fibrinogenolytic activities induced by snake venoms and isolated thrombin-like enzymes were partially inhibited. Furthermore, the potential use of these inhibitors to complement antivenom therapy as an alternative treatment and/or used as molecular models for development of new therapeutical agents in the treatment of snake bite envenomations needs to be evaluated in future studies.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Baccharis / chemistry
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Blood Coagulation / drug effects
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Carbohydrate Sequence
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Circular Dichroism
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Crotalid Venoms / enzymology
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Crotalid Venoms / toxicity
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Fibrin / chemistry
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Fibrinogen / chemistry
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Hemorrhage / chemically induced
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Hemorrhage / prevention & control
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Magnetic Resonance Spectroscopy
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Male
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Mice
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Molecular Sequence Data
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Phospholipases A / antagonists & inhibitors
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Phospholipases A / toxicity
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Plant Extracts / chemistry
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Plants / chemistry*
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Saponins / isolation & purification
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Saponins / pharmacology*
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Serine Proteinase Inhibitors / isolation & purification
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Serine Proteinase Inhibitors / pharmacology*
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Snake Venoms / enzymology*
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Snake Venoms / toxicity*
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Spectrophotometry, Ultraviolet
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Triterpenes / isolation & purification
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Triterpenes / pharmacology*
Substances
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Crotalid Venoms
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Plant Extracts
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Saponins
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Serine Proteinase Inhibitors
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Snake Venoms
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Triterpenes
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macrolobin A
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macrolobin B
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Fibrin
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Fibrinogen
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Phospholipases A