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Antimicrobial activity of myotoxic phospholipases A2 from crotalid snake venoms and synthetic peptide variants derived from their C-terminal region.
The bactericidal and anti-endotoxic properties of pEM-2, combined with its relatively low toxicity towards eukaryotic cells, highlight it as a promising candidate for further evaluation of its antimicrobial potential in vivo. Expand
Fungicidal activity of a phospholipase-A2-derived synthetic peptide variant against Candida albicans.
This peptide displays a broad-spectrum antimicrobial activity, in the absence of hemolytic activity, and the fungicidal action of pEM-2 against Candida can be partially inhibited by increasing concentrations of extracellular divalent cations, in agreement with its proposed membrane-permeabilizing mechanism of action. Expand
Bactericidal and Antiendotoxic Properties of Short Cationic Peptides Derived from a Snake Venom Lys49 Phospholipase A2
It is demonstrated that phospholipase A2-derived peptides may have the potential to counteract microbial infections and encourage further evaluations of their actions in vivo. Expand