New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
18375018
DOI
10.1016/j.peptides.2008.02.007
PII: S0196-9781(08)00078-8
Knihovny.cz E-resources
- MeSH
- Anti-Bacterial Agents chemical synthesis chemistry pharmacology MeSH
- Bacillus subtilis drug effects MeSH
- Cell Degranulation MeSH
- Erythrocytes drug effects MeSH
- Escherichia coli drug effects MeSH
- Hemolysis drug effects physiology MeSH
- Hydrophobic and Hydrophilic Interactions MeSH
- Inhibitory Concentration 50 MeSH
- Antimicrobial Cationic Peptides chemical synthesis chemistry pharmacology MeSH
- Rats MeSH
- Mast Cells drug effects physiology MeSH
- Microbial Sensitivity Tests MeSH
- Molecular Sequence Data MeSH
- Peptides chemical synthesis chemistry genetics isolation & purification pharmacology MeSH
- Pseudomonas aeruginosa drug effects MeSH
- Amino Acid Sequence MeSH
- Wasps chemistry MeSH
- Staphylococcus aureus drug effects MeSH
- Amino Acid Substitution MeSH
- Wasp Venoms chemistry genetics pharmacology MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Anti-Bacterial Agents MeSH
- Antimicrobial Cationic Peptides MeSH
- Peptides MeSH
- Wasp Venoms MeSH
Four new peptides of the mastoparan family, characterized recently in the venom of three neotropical social wasps collected in the Dominican Republic, Polistes major major, Polistes dorsalis dorsalis and Mischocyttarus phthisicus were synthesized and tested for antimicrobial potency against Bacillus subtilis, Staphylococcus aureus, Escherichia coli (E.c.) and Pseudomonas aeruginosa, and for hemolytic and mast cells degranulation activities. As these peptides possess strong antimicrobial activity (minimal inhibitory concentration (MIC) values against Bacillus subtillis and E.c. in the range of 5-40 microM), we prepared 40 of their analogs to correlate biological activities, especially antimicrobial, with the net positive charge, hydrophobicity, amphipathicity, peptide length, amino acid substitutions at different positions of the peptide chain, N-terminal acylation and C-terminal deamidation. Circular dichroism spectra of the peptides measured in the presence of trifluoroethanol or SDS showed that the peptides might adopt alpha-helical conformation in such anisotropic environments.
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