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
| Autor: | Manuel Humberto Mera López, Michelle Cruz Costa, Ana Carolina Martins Magalhães, Elisabeth F. Schwartz, Dágon Manoel Ribeiro, Beatriz Vasconcelos Ibituruna, Luana Cristina Camargo, Lucas Ferreira da Rocha, Gabriel Avohay Alves Campos, Mosar Corrêa Rodrigues, Lourival D. Possani, Luciana Marangni Nolli, Kamila Soares Lopes, Adolfo Carlos Barros de Souza, Alessa Bembom Garcia, Márcia Renata Mortari, Fernando Zamudio-Zuñiga |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Physiology Wasps Wasp Venoms Venom Peptide Biology Hemolysis Biochemistry 03 medical and health sciences Cellular and Molecular Neuroscience Endocrinology medicine Animals Humans Bioassay Trypsin Amino Acid Sequence EC50 Alanine chemistry.chemical_classification Vespidae medicine.disease biology.organism_classification Peptide Fragments Amino acid 030104 developmental biology chemistry Peptides Oligopeptides |
| Zdroj: | Peptides. 95:84-93 |
| ISSN: | 0196-9781 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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