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New potent antimicrobial peptides from the venom of Polistinae wasps and their analogs
V. Čeřovský, J. Slaninová, V. Fučík, H. Hulačová, L. Borovičková, R. Ježek, L. Bednárová
Language English Country United States
NLK
ScienceDirect (archiv)
from 1993-01-01 to 2009-12-31
- MeSH
- Anti-Bacterial Agents pharmacology chemical synthesis chemistry MeSH
- Bacillus subtilis drug effects MeSH
- Cell Degranulation MeSH
- Erythrocytes drug effects MeSH
- Escherichia coli drug effects MeSH
- Financing, Organized MeSH
- Hemolysis physiology drug effects MeSH
- Hydrophobic and Hydrophilic Interactions MeSH
- Inhibitory Concentration 50 MeSH
- Antimicrobial Cationic Peptides pharmacology chemical synthesis chemistry MeSH
- Rats MeSH
- Mast Cells physiology drug effects MeSH
- Microbial Sensitivity Tests MeSH
- Molecular Sequence Data MeSH
- Peptides pharmacology chemical synthesis chemistry isolation & purification drug effects MeSH
- Pseudomonas aeruginosa drug effects MeSH
- Amino Acid Sequence MeSH
- Wasps chemistry MeSH
- Staphylococcus aureus drug effects MeSH
- Amino Acid Substitution MeSH
- Wasp Venoms pharmacology genetics chemistry MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Animals 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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- $a Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo nam. 2, 166 10 Prague 6, Czech Republic. cerovsky@uochb.cas.cz
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- $a 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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