Characterization of two peptides isolated from the venom of social wasp Chartergellus communis (Hymenoptera: Vespidae): Influence of multiple alanine residues and C-terminal amidation on biological effects

• Published in: Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2017-09, Vol.95, p.84-93
• Main Authors: Lopes, Kamila Soares, Campos, Gabriel Avohay Alves, Camargo, Luana Cristina, de Souza, Adolfo Carlos Barros, Ibituruna, Beatriz Vasconcelos, Magalhães, Ana Carolina Martins, da Rocha, Lucas Ferreira, Garcia, Alessa Bembom, Rodrigues, Mosar Correa, Ribeiro, Dagon Manoel, Costa, Michelle Cruz, López, Manuel Humberto Mera, Nolli, Luciana Marangni, Zamudio-Zuniga, Fernando, Possani, Lourival Domingos, Schwartz, Elisabeth Ferroni, Mortari, Márcia Renata
• Format: Article
• Language: English
• Subjects: Alanine - chemistry; Algesia; Amino Acid Sequence - genetics; Animals; Edema; Hemolysis; Hemolysis - drug effects; Humans; Multiple alanine residues; Oligopeptides - chemistry; Peptide; Peptide Fragments - chemistry; Peptide Fragments - pharmacology; Peptides - chemistry; Peptides - genetics; Peptides - pharmacology; Trypsin - chemistry; Wasp venom; Wasp Venoms - chemistry; Wasp Venoms - genetics; Wasp Venoms - pharmacology; Wasps - chemistry; Wasps - genetics
• ISSN: 0196-9781; 1873-5169
• DOI: 10.1016/j.peptides.2017.07.012

•Two peptides were characterized from the venom of the social wasp C. communis.•First time that a wasp's peptide with multiple alanines in their sequence is shown.•Communis (INWKAILGKIGK) induced edema formation.•Communis-AAAA (INWKAILGKIGKAAAAVL-NH2) induced hyperalgesia and hemolysis.•Multiple alanines and c-terminal amidation should influence the biological effects. Chatergellus communis is a wasp species endemic to the neotropical region and its venom constituents have never been described. In this study, two peptides from C. communis venom, denominated Communis and Communis-AAAA, were chemically and biologically characterized. In respect to the chemical characterization, the following amino acid sequences and molecular masses were identified: Communis: Ile-Asn-Trp-Lys-Ala-Ile-Leu-Gly-Lys-Ile-Gly-Lys-COOH (1340.9Da) Communis-AAAA: Ile-Asn-Trp-Lys-Ala-Ile-Leu-Gly-Lys-Ile-Gly-Lys-Ala-Ala-Ala-Ala-Val-Xle-NH2 (1836.3Da). Furthermore, their biological effects were compared, accounting for the differences in structural characteristics between the two peptides. To this end, three biological assays were performed in order to evaluate the hyperalgesic, edematogenic and hemolytic effects of these molecules. Communis-AAAA, unlike Communis, showed a potent hemolytic activity with EC50=142.6μM. Moreover, the highest dose of Communis-AAAA (2nmol/animal) induced hyperalgesia in mice. On the other hand, Communis (10nmol/animal) was able to induce edema but did not present hemolytic or hyperalgesic activity. Although both peptides have similarities in linear structures, we demonstrated the distinct biological effects of Communis and Communis-AAAA. This is the first study with Chartegellus communis venom, and both Communis and Communis-AAAA are unpublished peptides.