Journal
BIOLOGICAL & PHARMACEUTICAL BULLETIN
Volume 29, Issue 12, Pages 2493-2497Publisher
PHARMACEUTICAL SOC JAPAN
DOI: 10.1248/bpb.29.2493
Keywords
venom; wasp; polistes-mastoparan; polistes-protonectin; heamolytic acitivity; histamine-releasing activity
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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 VIS 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-Thr(6)-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 polistes-protonectin 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.
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