Fungicidal activity of a phospholipase A2-derived synthetic peptide variant against Candida albicans
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| Autores: | , , , , |
|---|---|
| Formato: | artículo original |
| Fecha de Publicación: | 2007 |
| Descripción: | pEM-2, a 13-mer synthetic peptide variant derived from myotoxin II, a phospholipase A2 homologue present in Bothrops asper snake venom, has shown potent bactericidal activity in previous studies due to the combination of cationic and hydrophobic amino acids, including three tryptophan-substituted residues in its sequence. This study reports that pEM-2 also exerts potent fungicidal activity against a variety of clinically relevant Candida species, killing 100% of yeasts at concentrations near 10 mg/l (5 μM), as indicated by plate counting assays. Thus, this peptide displays a broad-spectrum antimicrobial activity, in the absence of hemolytic activity. The fungicidal action of pEM-2 against Candida can be partially inhibited by increasing concentrations of extracellular divalent cations (Ca+2 or Mg+2), in agreement with its proposed membrane- permeabilizing mechanism of action. |
| País: | Kérwá |
| Institución: | Universidad de Costa Rica |
| Repositorio: | Kérwá |
| OAI Identifier: | oai:kerwa.ucr.ac.cr:10669/74286 |
| Acceso en línea: | http://seq.es/wp-content/uploads/2008/08/seq.es_seq_0214-3429_20_3_murillo.pdf https://hdl.handle.net/10669/74286 |
| Palabra clave: | Fungicidal Microbicidal Synthetic peptide Candida Phospholipase A2 Fungicida Microbicida Péptido sintético Fosfolipasa A2 |