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Biochemistry and toxicology of toxins purified from the venom of the snake Bothrops asper
(2009-12-01)
The isolation and study of individual snake venom components paves the way for a deeper
understanding of the pathophysiology of envenomings – thus potentially contributing to
improved therapeutic modalities in the clinical ...
Synthetic peptides derived from the C-terminal region of Lys49 phospholipase A2 homologues from Viperidae snake venoms: biomimetic activities and potential applications
(2010)
Lys49-phospholipase A2 homologues constitute a large family of toxins present in the venoms of viperid snake species, which
despite lacking catalytic activity, cause significant skeletal muscle necrosis. The main structural ...
Isolation, characterization and molecular cloning of AnMIP, a new α-type phospholipase A2 myotoxin inhibitor from the plasma of the snake Atropoides nummifer (Viperidae: Crotalinae)
(2007)
A new phospholipase A2 (PLA2)-inhibitory protein was isolated from the plasma of Atropoides nummifer, a crotaline snake from Central
America. This inhibitor was named AnMIP, given its ability to neutralize the activity ...
Antimicrobial activity of myotoxic phospholipases A2 from crotalid snake venoms and synthetic peptide variants derived from their C-terminal region
(2005)
A short peptide derived from the C-terminal region of Bothrops asper myotoxin II, a Lys49 phospholipase A2 (PLA2), was
previously found to reproduce the bactericidal activity of its parent molecule. In this study, a panel ...
Structure of myotoxin-II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
(2006)
Lys49 snake-venom phospholipase A2 (PLA2) homologues are highly myotoxic
proteins which, although lacking catalytic activity, possess the ability to disrupt
biological membranes, inducing significant muscle-tissue loss ...
Tyr→Trp-substituted peptide 115-129 of a Lys49 phospholipase A2 expresses enhanced membrane-damaging activities and reproduces its in vivo myotoxic effect
(1999)
Myotoxin II is a group II Lys49 phospholipase A2 (PLA2) isolated from the venom of the snake Bothrops asper. Previous
studies on a synthetic peptide derived from its heparin-binding, cationic/hydrophobic sequence 115^129 ...
Inhibitory effect of fucoidan on the activities of crotaline snake venom myotoxic phospholipases A2
(2003)
Myotoxic phospholipases A2 account for most of the muscle necrosis that results from envenenomation by crotaline snakes. In this study,
we investigated the protective effect of fucoidan, a natural sulfated polysaccharide ...
Comparative study of synthetic peptides corresponding to region 115-129 in Lys49 myotoxic phospholipases A2 from snake venoms
(2003)
Lys49 phospholipase A2 homologues constitute a group of catalytically-inactive proteins, present in the venoms of many
crotalid snakes, which induce myonecrosis. Current evidence supports the mapping of their toxic site ...
Crystallization of the Lys49 PLA2 homologue, myotoxin II from the venom of Atropoides nummifer
(2004-12)
Myotoxin II, a Lys49 catalytically inactive phospholipase A2 homologue from Atropoides nummifer venom, was purified, characterized
and crystallized. The crystals belongs to the tetragonal system, space group P43212, with ...