Abstract
Three novel peptides designated as PMM1, PMM2, and PMM3 were isolated and characterized from the venom of the social wasp Polistes major major, one of the most common wasps in the Dominican Republic. By Edman degradation, and MALDI‐TOF and ESI‐QTOF mass spectrometry, the primary sequences of these peptides were established as follows: PMM1, H‐Lys‐Arg‐Arg‐Pro‐Pro‐Gly‐Phe‐Thr‐Pro‐Phe‐Arg‐OH (1357.77 Da); PMM2, H‐Ile‐Asn‐Trp‐Lys‐Lys‐Ile‐Ala‐Ser‐Ile‐Gly‐Lys‐Glu‐Val‐Leu‐Lys‐Ala‐Leu‐NH~2~ (1909.19 Da); and PMM3, H‐Phe‐Leu‐Ser‐Ala‐Leu‐Leu‐Gly‐Met‐Leu‐Lys‐Asn‐Leu‐NH~2~ (1317.78 Da). The suggested sequences were confirmed by MS analysis of peptide fragments obtained by enzymatic digestion. The peptide PMM1 is a lysyl‐arginyl‐Thr^6^‐bradykinine that belongs to the wasp kinins group. The sequence of the PMM2 peptide is unique; it resembles somewhat the tetradecapeptide amides of the mastoparan group; however, the chain is extended by three additional amino acid residues. The sequence of PMM3 dodecapeptide is homologous to the peptides of the wasp chemotactic group. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.