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Toxins 2019, 11(3), 155; https://doi.org/10.3390/toxins11030155

New Mastoparan Peptides in the Venom of the Solitary Eumenine Wasp Eumenes micado

1
Institute of Natural Medicine, University of Toyama, Toyama, Toyama 930-0194, Japan
2
Immunopathology Laboratory, Butantan Institute, Sao Paulo SP 05503-900, Brazil
3
Laboratory of Physiology and Animal Toxins, Federal University of West Pará, Santarém PA 68040-070, Brazil
4
Department of Biological Sciences, State University of Santa Cruz, Ilhéus BA 45662-900, Brazil
5
Research Center for Medicinal Plant Resources, National Institutes of Biomedical Innovation, Health and Nutrition, Tsukuba, Ibaraki 305-0843, Japan
6
Department of Molecular and Pharmacological Neuroscience, Graduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima, Hiroshima 734-8551, Japan
7
Laboratory of Microbial Chemistry, School of Pharmacy, Kitasato University, Minato-ku, Tokyo 108-8641, Japan
8
Department of Pharmacology, Hiroshima University Graduate School of Biomedical & Health Sciences, Hiroshima 734-8553, Japan
*
Author to whom correspondence should be addressed.
Present address: Eco-Frontier Center of Medicinal Resources, School of Pharmacy, Kumamoto University, Kumamoto, Kumamoto 862-0973, Japan.
Received: 12 January 2019 / Revised: 28 February 2019 / Accepted: 5 March 2019 / Published: 10 March 2019
(This article belongs to the Special Issue Toxins-Membrane Interactions)
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Abstract

Comprehensive LC-MS and MS/MS analysis of the crude venom extract from the solitary eumenine wasp Eumenes micado revealed the component profile of this venom mostly consisted of small peptides. The major peptide components, eumenine mastoparan-EM1 (EMP-EM1: LKLMGIVKKVLGAL-NH2) and eumenine mastoparan-EM2 (EMP-EM2: LKLLGIVKKVLGAI-NH2), were purified and characterized by the conventional method. The sequences of these new peptides are homologous to mastoparans, the mast cell degranulating peptides from social wasp venoms; they are 14 amino acid residues in length, rich in hydrophobic and basic amino acids, and C-terminal amidated. Accordingly, these new peptides can belong to mastoparan peptides (in other words, linear cationic α-helical peptides). Indeed, the CD spectra of these new peptides showed predominantly α-helix conformation in TFE and SDS. In biological evaluation, both peptides exhibited potent antibacterial activity, moderate degranulation activity from rat peritoneal mast cells, and significant leishmanicidal activity, while they showed virtually no hemolytic activity on human or mouse erythrocytes. These results indicated that EMP-EM peptides rather strongly associated with bacterial cell membranes rather than mammalian cell membranes. View Full-Text
Keywords: solitary wasp; venom; mastoparan peptide; linear cationic α-helical peptide; amphipathic α-helix structure. solitary wasp; venom; mastoparan peptide; linear cationic α-helical peptide; amphipathic α-helix structure.
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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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Konno, K.; Kazuma, K.; Rangel, M.; Stolarz-de-Oliveira, J.; Fontana, R.; Kawano, M.; Fuchino, H.; Hide, I.; Yasuhara, T.; Nakata, Y. New Mastoparan Peptides in the Venom of the Solitary Eumenine Wasp Eumenes micado. Toxins 2019, 11, 155.

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