Melectin: a novel antimicrobial peptide from the venom of the cleptoparasitic bee Melecta albifrons
Language English Country Germany Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Anti-Bacterial Agents chemical synthesis isolation & purification pharmacology MeSH
- Circular Dichroism MeSH
- Cell Degranulation drug effects MeSH
- Erythrocytes drug effects MeSH
- Gram-Negative Bacteria drug effects MeSH
- Gram-Positive Bacteria drug effects MeSH
- Hemolysis drug effects MeSH
- Hydrophobic and Hydrophilic Interactions MeSH
- Inhibitory Concentration 50 MeSH
- Antimicrobial Cationic Peptides chemical synthesis isolation & purification pharmacology MeSH
- Rats MeSH
- Mast Cells drug effects physiology MeSH
- Microbial Sensitivity Tests MeSH
- Molecular Sequence Data MeSH
- Rats, Wistar MeSH
- Protein Structure, Secondary MeSH
- Amino Acid Sequence MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
- Bee Venoms chemistry MeSH
- Bees * MeSH
- Chromatography, High Pressure Liquid 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
- melectin MeSH Browser
- Bee Venoms MeSH
A novel antimicrobial peptide designated melectin was isolated from the venom of the cleptoparasitic bee Melecta albifrons. Its primary sequence was established as H-Gly-Phe-Leu-Ser-Ile-Leu-Lys-Lys-Val-Leu-Pro-Lys-Val-Met-Ala-His-Met-Lys-NH(2) by Edman degradation and ESI-QTOF mass spectrometry. Synthetic melectin exhibited antimicrobial activity against both gram-positive and -negative bacteria and it degranulated rat peritoneal mast cells, but its hemolytic activity was low. The CD spectra of melectin measured in the presence of trifluoroethanol and sodium dodecyl sulfate showed a high content alpha-helices, which indicates that melectin can adopt an amphipathic alpha-helical secondary structure in an anisotropic environment such as the bacterial cell membrane. To envisage the role of the proline residue located in the middle of the peptide chain on biological activity and secondary structure, we prepared several melectin analogues in which the Pro11 residue was either replaced by other amino acid residues or was omitted. The results of biological testing suggest that a Pro kink in the alpha-helical structure of melectin plays an important role in selectivity for bacterial cells. In addition, a series of N- and C-terminal-shortened analogues was synthesized to examine which region of the peptide is related to antimicrobial activity.
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