Antibacterial and antifungal properties of alpha-helical, cationic peptides in the venom of scorpions from southern Africa
| Autor: | Leentje, Moerman, Suzanne, Bosteels, Wim, Noppe, Jean, Willems, Elke, Clynen, Liliane, Schoofs, Karin, Thevissen, Jan, Tytgat, Johan, Van Eldere, Jurg, Van Der Walt, Fons, Verdonck |
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| Rok vydání: | 2002 |
| Předmět: |
Antifungal Agents
Sequence Homology Amino Acid Molecular Sequence Data Fungi Scorpion Venoms Wasp Venoms In Vitro Techniques Gram-Positive Bacteria Hemolysis Melitten Africa Southern Protein Structure Secondary Molecular Weight Gram-Negative Bacteria Animals Humans Intercellular Signaling Peptides and Proteins Amino Acid Sequence Peptides Antimicrobial Cationic Peptides |
| Zdroj: | European journal of biochemistry. 269(19) |
| ISSN: | 0014-2956 |
| Popis: | Two novel pore-forming peptides have been isolated from the venom of the South-African scorpion Opistophtalmus carinatus. These peptides, designated opistoporin 1 and 2, differ by only one amino acid and belong to a group of alpha-helical, cationic peptides. For the first time, a comparison of the primary structures of alpha-helical pore-forming peptides from scorpion venom was undertaken. This analysis revealed that peptides in the range of 40-50 amino acids contain a typical scorpion conserved sequence S(x)3KxWxS(x)5L. An extensive study of biological activity of synthesized opistoporin 1 and parabutoporin, a pore-forming peptide previously isolated from the venom of the South-African scorpion Parabuthus schlechteri, was undertaken to investigate an eventual cell-selective effect of the peptides. Opistoporin 1 and parabutoporin were most active in inhibiting growth of Gram-negative bacteria (1.3-25 micro m), while melittin and mastoparan, two well-known cytolytic peptides, were more effective against Gram-positive bacteria in the same concentration range. In addition, the peptides showed synergistic activity with some antibiotics commonly used in therapy. Opistoporin 1 and parabutoporin had hemolytic activity intermediate between the least potent mastoparan and the highly lytic melittin. Furthermore, all peptides inhibited growth of fungi. Experiments with SYTOX green suggested that this effect is related to membrane permeabilization. |
| Databáze: | OpenAIRE |
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