Chemical and biological characterization of four new linear cationic α-helical peptides from the venoms of two solitary eumenine wasps

Four novel peptides were isolated from the venoms of the solitary eumenine wasps Eumenes rubrofemoratus and Eumenes fraterculus. Their sequences were determined by MALDI-TOF/TOF (matrix assisted laser desorption/ionization time-of-flight mass spectrometry) analysis, Edman degradation and solid-phase...

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Bibliographic Details
Published in:Toxicon (Oxford) 2011-06, Vol.57 (7-8), p.1081-1092
Main Authors: Rangel, Marisa, dos Santos Cabrera, Marcia Perez, Kazuma, Kohei, Ando, Kenji, Wang, Xiaoyu, Kato, Manabu, Nihei, Ken-ichi, Hirata, Izaura Yoshico, Cross, Tyra J., Garcia, Angélica Nunes, Faquim-Mauro, Eliana L., Franzolin, Marcia Regina, Fuchino, Hiroyuki, Mori-Yasumoto, Kanami, Sekita, Setsuko, Kadowaki, Makoto, Satake, Motoyoshi, Konno, Katsuhiro
Format: Article
Language:English
Subjects:
Amino Acid Sequence
amino acids
Amphipathic α-helix structure
Animal poisons toxicology. Antivenoms
Animals
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - pharmacology
anti-infective properties
Antimicrobial activity
antimicrobial peptides
Biological and medical sciences
Cations - chemistry
Circular Dichroism
desorption
disulfide bonds
Eumenes
hemolysis
hydrophobicity
Hymenoptera
ionization
Linear cationic α-helical peptide
Mass Spectrometry
Medical sciences
Molecular Sequence Data
Peptides - chemistry
Peptides - isolation & purification
Peptides - pharmacology
Protein Structure, Secondary
sodium dodecyl sulfate
Solitary wasp
Toxicology
venoms
Venoms - chemistry
Venoms - pharmacology
Wasps - chemistry
Wasps - metabolism
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Summary:Four novel peptides were isolated from the venoms of the solitary eumenine wasps Eumenes rubrofemoratus and Eumenes fraterculus. Their sequences were determined by MALDI-TOF/TOF (matrix assisted laser desorption/ionization time-of-flight mass spectrometry) analysis, Edman degradation and solid-phase synthesis. Two of them, eumenitin-R (LNLKGLIKKVASLLN) and eumenitin-F (LNLKGLFKKVASLLT), are highly homologous to eumenitin, an antimicrobial peptide from a solitary eumenine wasp, whereas the other two, EMP-ER (FDIMGLIKKVAGAL-NH2) and EMP-EF (FDVMGIIKKIAGAL-NH2), are similar to eumenine mastoparan-AF (EMP-AF), a mast cell degranulating peptide from a solitary eumenine wasp. These sequences have the characteristic features of linear cationic cytolytic peptides; rich in hydrophobic and basic amino acids with no disulfide bond, and accordingly, they can be predicted to adopt an amphipathic α-helix secondary structure. In fact, the CD (circular dichroism) spectra of these peptides showed significant α-helical conformation content in the presence of TFE (trifluoroethanol), SDS (sodium dodecylsulfate) and asolectin vesicles. In the biological evaluation, all the peptides exhibited a significant broad-spectrum antimicrobial activity, and moderate mast cell degranulation and leishmanicidal activities, but showed virtually no hemolytic activity. ► Four novel peptides were isolated from the venoms of the solitary eumenine wasps. ► The sequences have the characteristic features of linear cationic α-helical peptides. ► All the peptides exhibited antimicrobial, mast cell degranulation and leishmanicidal activities, but virtually no hemolytic activity.
ISSN:0041-0101
1879-3150
DOI:10.1016/j.toxicon.2011.04.014