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Toxins 2016, 8(3), 61; doi:10.3390/toxins8030061

Paulistine—The Functional Duality of a Wasp Venom Peptide Toxin

1
Department of Biology/Center of Study of Social Insects, Institute of Biosciences, São Paulo State University (UNESP), Rio Claro 13506-900, SP, Brazil
2
Fundação Oswaldo Cruz—Health Ministry/Fiocruz Rondônia, Porto Velho 21040-900, RO, Brazil
3
Department of Clinical Analysis, Proteomic Center, Faculty of Pharmaceutical, Sciences, São Paulo State University (UNESP), Araraquara 14801-902, SP, Brazil
*
Author to whom correspondence should be addressed.
Academic Editor: Glenn F. King
Received: 9 December 2015 / Revised: 12 February 2016 / Accepted: 22 February 2016 / Published: 29 February 2016
(This article belongs to the Special Issue Arthropod Venoms)
View Full-Text   |   Download PDF [3518 KB, uploaded 29 February 2016]   |  

Abstract

It has been reported that Paulistine in the venom of the wasp Polybia paulista co-exists as two different forms: an oxidized form presenting a compact structure due to the presence of a disulfide bridge, which causes inflammation through an apparent interaction with receptors in the 5-lipoxygenase pathway, and a naturally reduced form (without the disulfide bridge) that exists in a linear conformation and which also causes hyperalgesia and acts in the cyclooxygenase type II pathway. The reduced peptide was acetamidomethylated (Acm-Paulistine) to stabilize this form, and it still maintained its typical inflammatory activity. Oxidized Paulistine docks onto PGHS2 (COX-2) molecules, blocking the access of oxygen to the heme group and inhibiting the inflammatory activity of Acm-Paulistine in the cyclooxygenase type II pathway. Docking simulations revealed that the site of the docking of Paulistine within the PGHS2 molecule is unusual among commercial inhibitors of the enzyme, with an affinity potentially much higher than those observed for traditional anti-inflammatory drugs. Therefore, Paulistine causes inflammatory activity at the level of the 5-lipooxygenase pathway and, in parallel, it competes with its reduced form in relation to the activation of the cyclooxygenase pathway. Thus, while the reduced Paulistine causes inflammation, its oxidized form is a potent inhibitor of this activity. View Full-Text
Keywords: wasp venom; inflammation; pain; peptide synthesis; molecular modeling; docking wasp venom; inflammation; pain; peptide synthesis; molecular modeling; docking
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Arcuri, H.A.; Gomes, P.C.; de Souza, B.M.; Dias, N.B.; Brigatte, P.; Stabeli, R.G.; Palma, M.S. Paulistine—The Functional Duality of a Wasp Venom Peptide Toxin. Toxins 2016, 8, 61.

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