Novel biologically active peptides from the venom of Polistes rothneyi iwatai.
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, Thr6-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 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.
Murata
Kazuya
K
Graduate School of Science, Osaka City University, Japan.
Shinada
Tetsuro
T
Ohfune
Yasufumi
Y
Hisada
Miki
M
Yasuda
Akikazu
A
Naoki
Hideo
H
Nakajima
Terumi
T
D000595:Amino Acid Sequence; D000818:Animals; D002478:Cells, Cultured; D002851:Chromatography, High Pressure Liquid; D005260:Female; D006636:Histamine Release / Q000187:drug effects; D008969:Molecular Sequence Data; D010455:Peptides / Q000302:isolation & purification / Q000494:pharmacology*; D051381:Rats; D021241:Spectrometry, Mass, Electrospray Ionization; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014862:Wasp Venoms / Q000737:chemistry*
D010455:Peptides; D014862:Wasp Venoms