Structural and biological characterization of three novel mastoparan peptides from the venom of the neotropical social wasp Protopolybia exigua (Saussure)
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Data
2005-01-01
Autores
Mendes, M. A.
de Souza, B. M.
Palma, Mario Sergio [UNESP]
Título da Revista
ISSN da Revista
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Editor
Elsevier B.V.
Resumo
The venom of the Neotropical social wasp Protopolybia exigua(Saussure) was fractionated by RP-HPLC resulting in the elution of 20 fractions. The homogeneity of the preparations were checked out by using ESI-MS analysis and the fractions 15, 17 and 19 (eluted at the most hydrophobic conditions) were enough pure to be sequenced by Edman degradation chemistry, resulting in the following sequences:Protopolybia MPI I-N-W-L-K-L-G-K-K-V-S-A-I-L-NH2 Protopolybia-MP II I-N-W-K-A-I-I-E-A-A-K-Q-A-L-NH2 Protopolybia-MP III I-N-W-L-K-L-G-K-A-V-I-D-A-L-NH2All the peptides were manually synthesized on-solid phase and functionally characterized. Protopolybia-MP I is a hemolytic mastoparan, probably acting on mast cells by assembling in plasma membrane, resulting in pore formation; meanwhile, the peptides Protopolybia-MP II and -MP III were characterized as a non-hemolytic mast cell degranulator toxins, which apparently act by virtue of their binding to G-protein receptor, activating the mast cell degranulation. (C) 2004 Elsevier Ltd. All rights reserved.
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Palavras-chave
social wasp, mastoparan, hemolysis, antimicrobial peptide, G-protein receptor
Como citar
Toxicon. Oxford: Pergamon-Elsevier B.V., v. 45, n. 1, p. 101-106, 2005.