Triterpenoid saponins, new metalloprotease snake venom inhibitors isolated from Pentaclethra macroloba
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:
-
Toxicon
- Pub Date:
- January 2007
- DOI:
- Bibcode:
- 2007Txcn...50..283D
- Keywords:
-
- Batx;
- Bothrops atrox venom;
- Basp;
- B. asper venom;
- Balt;
- B. alternatus venom;
- Bjar;
- B. jararaca venom;
- Bjussu;
- B. jararacussu venom;
- BjussuMP-I;
- B. jararacussu metalloprotease I;
- Bmoo;
- B. moojeni venom;
- Bneu;
- B. neuwiedi venom;
- Bpir;
- B. pirajai venom;
- Catx;
- Crotalus atrox venom;
- Cdt;
- C. durissus terrificus venom;
- Crho;
- Calloselasma rhodostoma venom;
- CK;
- creatine kinase;
- EPema;
- aqueous extract of Pentaclethra macroloba;
- Macrolobin A;
- Pentaclethra macroloba triterpenoid saponin A;
- Macrolobin B;
- Pentaclethra macroloba triterpenoid saponin B;
- PBS;
- phosphate-buffered saline;
- Pentaclethra macroloba;
- Triterpenoid saponins;
- Antivenom Brazilian plants;
- Antihemorrhagic and antiproteolytic activity;
- Proteases