Abstract
The present study reports the structural characteristics, the biological activities, and preliminary clinical investigations of three synthetic members of the dermaseptin family of antimicrobial peptides. The three peptides showed similar tendencies to form alpha-helical structures in non-polar media. The antimicrobial activity towards bacteria and fungi was determined in the micromolar concentration and the peptides did not influenced peritoneal cells viability. One of the peptides was intravenously administered in mice at concentrations similar to those of antibiotics employed in bacterial/fungal infections and it did not cause any detectable changes in cells and tissues.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Amphibian Proteins / chemistry*
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Amphibian Proteins / metabolism
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Amphibian Proteins / toxicity*
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Animals
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Antimicrobial Cationic Peptides / chemistry*
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Antimicrobial Cationic Peptides / metabolism
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Antimicrobial Cationic Peptides / toxicity*
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Anura
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Candida albicans / drug effects*
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Candida tropicalis / drug effects
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Cell Survival / drug effects
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Circular Dichroism
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Dose-Response Relationship, Drug
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Leukocyte Count
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Mice
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Microbial Sensitivity Tests
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Molecular Sequence Data
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Nocardia / drug effects
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Peritoneum / cytology*
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Protein Structure, Secondary
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Staphylococcus aureus / drug effects
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Streptococcus / drug effects*
Substances
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Amphibian Proteins
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Antimicrobial Cationic Peptides
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dermadistinctin K, Phyllomedusa distincta
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dermaseptin