Journal
AMINO ACIDS
Volume 37, Issue 2, Pages 389-394Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-008-0166-y
Keywords
Solitary wasp; Mass spectrometry; Mastoparan; Protonectin; Hemolytic activity
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Funding
- Research for the Future Program from the Japan Society for the Promotion of Science [JSPS 99L01204]
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Two novel biologically active peptides, Eumenine mastoparan-OD and Orancis-Protonectin, were isolated from a solitary wasp, Orancistrocerus drewseni drewseni (Eumeninae, Vespidae). MALDI-TOF MS analysis of a small amount of the crude venom gave two intensive molecular-related ion peaks at m/z 1269.9 and 1552.9 that were expected to be novel based on a peptide database search. Purification of the crude venom by HPLC gave two peptide fractions, P-1 and P-2. The amino acid sequence of P-1 (GRILSFIKAGLAEHL-NH2) and P-2 (ILGIITSLLKSL-NH2) were determined by ESI-MS/MS, automated Edman degradation, and amino acid analysis. According to the high sequence homology with those of mastoparan and protonectin, P-1 and P-2 were labeled Eumenine mastoparan-OD and Orancis-Protonectin, respectively. Orancis-Protonectin is the first example of a protonectin analog isolated from the venom of a solitary wasp. The hemolytic activities of these new peptides were more potent than that of mastoparan.
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