Four novel peptides, polistes-mastoparan-R1, 2, 3, and polistes- protonectin, were isolated from the venom of a paper wasp, Polistes rothneyi iwatai. MALDI-TOF MS analysis of a small amount of the crude venom gave six molecular-related ion peaks. Among them, m/z 1565 was expected to be a novel peptide. Purification of the crude venom by HPLC gave two known kinins, Thr 6-bradykinin and Ala-Arg-Thr6-bradykinin, and four novel peptides named polistes-mastoparan-R1, 2, and 3, and polistes-protonectin. Polistes-mastoparan-R1, 2, and 3 (Pm-R) were tetradecapeptides that possess high sequence homology with that of mastoparan. The sequence of polistesprotonectin was similar to that of protonectin isolated from a Brazilian paper wasp. Histamine-releasing activities of Pm-R1, 2, and 3 were more potent than that of mastoparan. Polistes-protonectin exhibited the most potent hemolytic activity in comparison with the four novel peptides and mastoparan. © 2006 Pharmaceutical Society of Japan.
CITATION STYLE
Murata, K., Shinada, T., Ohfune, Y., Hisada, M., Yasuda, A., Naoki, H., & Nakajima, T. (2006). Novel biologically active peptides from the venom of Polistes rothneyi iwatai. Biological and Pharmaceutical Bulletin, 29(12), 2493–2497. https://doi.org/10.1248/bpb.29.2493
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