Novel antimicrobial peptides from the venom of the eusocial bee Halictus sexcinctus (Hymenoptera: Halictidae) and their analogs
Language English Country Austria Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Anti-Bacterial Agents chemistry isolation & purification pharmacology MeSH
- Bacteria drug effects MeSH
- Erythrocytes drug effects MeSH
- Hemolysis drug effects MeSH
- Hemolysin Proteins chemistry isolation & purification pharmacology MeSH
- Antimicrobial Cationic Peptides chemistry isolation & purification pharmacology MeSH
- Rats MeSH
- Molecular Sequence Data MeSH
- Protein Structure, Secondary MeSH
- Amino Acid Sequence MeSH
- Bee Venoms chemistry MeSH
- Bees chemistry 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
- Hemolysin Proteins MeSH
- Antimicrobial Cationic Peptides MeSH
- Bee Venoms MeSH
Two novel antimicrobial peptides, named halictines, were isolated from the venom of the eusocial bee Halictus sexcinctus. Their primary sequences were established by ESI-QTOF mass spectrometry, Edman degradation and enzymatic digestion as Gly-Met-Trp-Ser-Lys-Ile-Leu-Gly-His-Leu-Ile-Arg-NH2 (HAL-1), and Gly-Lys-Trp-Met-Ser-Leu-Leu-Lys-His-Ile-Leu-Lys-NH2 (HAL-2). Both peptides exhibited potent antimicrobial activity against Gram-positive and Gram-negative bacteria but also noticeable hemolytic activity. The CD spectra of HAL-1 and HAL-2 measured in the presence of trifluoroethanol or SDS showed ability to form an amphipathic alpha-helical secondary structure in an anisotropic environment such as bacterial cell membrane. NMR spectra of HAL-1 and HAL-2 measured in trifluoroethanol/water confirmed formation of helical conformation in both peptides with a slightly higher helical propensity in HAL-1. Altogether, we prepared 51 of HAL-1 and HAL-2 analogs to study the effect of such structural parameters as cationicity, hydrophobicity, alpha-helicity, amphipathicity, and truncation on antimicrobial and hemolytic activities. The potentially most promising analogs in both series are those with increased net positive charge, in which the suitable amino acid residues were replaced by Lys. This improvement basically relates to the increase of antimicrobial activity against pathogenic Pseudomonas aeruginosa and to the mitigation of hemolytic activity.
References provided by Crossref.org
Polymer-Antimicrobial Peptide Constructs with Tailored Drug-Release Behavior
Interaction of Halictine-Related Antimicrobial Peptides with Membrane Models
