Premium
Identification of three novel peptides isolated from the venom of the neotropical social wasp Polistes major major
Author(s) -
ČeŘovský Václav,
Pohl Jan,
Yang Zhihua,
Alam Naseer,
Attygalle Athula B.
Publication year - 2007
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.860
Subject(s) - edman degradation , peptide , venom , mastoparan , peptide sequence , chemistry , biochemistry , amino acid , stereochemistry , gene , g protein , receptor
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.