dc.contributorUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T13:55:17Z
dc.date.available2014-05-20T13:55:17Z
dc.date.created2014-05-20T13:55:17Z
dc.date.issued2011-09-06
dc.identifierJournal of Proteomics. Amsterdam: Elsevier B.V., v. 74, n. 10, p. 2123-2137, 2011.
dc.identifier1874-3919
dc.identifierhttp://hdl.handle.net/11449/19783
dc.identifier10.1016/j.jprot.2011.06.004
dc.identifierWOS:000295302800027
dc.identifier2901888624506535
dc.description.abstractThe wasp Agelaia pallipes pallipes is one of the most aggressive species from the neotropical region, causing many stinging accidents every year, characterized by severe envenoming reactions. The identification of peptides is important for understanding the envenoming process; however, the tiny amount of venom produced by these insects makes this task a challenge, using classical analytical approaches. Thus, the venom was previously fractionated, and the sequences were obtained through the use of electrospray ionization with a tridimensional ion-trap and time-of-flight mass analysis under CID conditions. This approach permitted the sequence assignment of nine peptides. The presence of type -d and -w ions generated from the fragmentation of the side chains was used to resolve I/L ambiguity. The distinction between K and Q residues was achieved through esterification of the alpha- and epsilon-amino groups in the peptides, followed by mass spectrometry analysis. Six of these peptides were short, linear and polycationic, while the three other peptides presented a single disulfide bridge. The use of reduction and alkylation protocols, followed by ESI-IT-TOF/MS analysis under CID conditions, permitted easy sequencing of the three peptides presenting this post-translational modification. These peptides presented activity related to mast cell degranulation, hemolysis, or even the chemotaxis of leukocytes. (C) 2011 Elsevier B.V. All rights reserved.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationJournal of Proteomics
dc.relation3.722
dc.relation1,430
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectPeptidomics
dc.subjectRP-HPLC
dc.subjectESI-IT-TOF/MS
dc.subjectPolycationic peptides
dc.subjectWasp venom
dc.titleProfiling the peptidome of the venom from the social wasp Agelaia pallipes pallipes
dc.typeArtículos de revistas


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