Eumenitin, a novel antimicrobial peptide from the venom of the solitary eumenine wasp Eumenes rubronotatus
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Data
2006-11-01
Autores
Konno, Katsuhiro
Hisada, Miki
Naoki, Hideo
Itagaki, Yasuhiro
Fontana, Renato
Rangel, Marisa
Stolarz Oliveira, Joacir
Perez dos Santos Cabreraf, Marcia
Ruggiero Neto, Joao
Hide, Izumi
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Editor
Elsevier B.V.
Resumo
A novel antimicrobial peptide, eumenitin, was isolated from the venom of the solitary eumenine wasp Eumenes rubronotatus. The sequence of eumenitin, Leu-Asn-Leu-Lys-Gly-Ile-Phe-Lys-Lys-Val-Ala-Ser-Leu-Leu-Thr, was mostly analyzed by mass spectrometry together with Edman degradation, and corroborated by solid-phase synthesis. This peptide has characteristic features of cationic linear a-helical antimicrobial peptides, and therefore, can be predicted to adopt an amphipathic a-helix secondary structure. In fact, the CD spectra of eumenitin in the presence of TFE or SDS showed a high content of alpha-helical conformation. Eumenitin exhibited inhibitory activity against both Gram-positive and Gram-negative bacteria, and moderately stimulated degranulation from the rat peritoneal mast cells and the RBL-2H3 cells, but showed no hemolytic activity against human erythrocytes. This antimicrobial peptide in the eumenine wasp venom may play a role in preventing potential infection by microorganisms during prey consumption by their larvae. (c) 2006 Elsevier B.V. All rights reserved.
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eumenitin, solitary wasp venom, antimicrobial peptide, cationic linear alpha-helical peptide, amphipathic alpha-helix structure
Como citar
Peptides. New York: Elsevier B.V., v. 27, n. 11, p. 2624-2631, 2006.