Chemical and biological characterization of four new linear cationic alpha-helical peptides from the venoms of two solitary eumenine wasps

Chemical and biological characterization of four new linear cationic alpha-helical peptides from the venoms of two solitary eumenine wasps

Author Rangel, Marisa Google Scholar
Santos Cabrera, Marcia Perez dos Google Scholar
Kazuma, Kohei Google Scholar
Ando, Kenji Google Scholar
Wang, Xiaoyu Google Scholar
Kato, Manabu Google Scholar
Nihei, Ken-ichi Google Scholar
Hirata, Izaura Yoshico Autor UNIFESP Google Scholar
Cross, Tyra J. Google Scholar
Garcia, Angelica Nunes Google Scholar
Faquim-Mauro, Eliana L. Google Scholar
Franzolin, Marcia Regina Google Scholar
Fuchino, Hiroyuki Google Scholar
Mori-Yasumoto, Kanami Google Scholar
Sekita, Setsuko Google Scholar
Kadowaki, Makoto Google Scholar
Satake, Motoyoshi Google Scholar
Konno, Katsuhiro Google Scholar
Institution Toyama Univ
Butantan Inst
São Paulo State Univ
Yamada Apiculture Ctr Inc
Utsunomiya Univ
Universidade Federal de São Paulo (UNIFESP)
Univ Victoria
Natl Inst Biomed Innovat
Tokushima Bunri Univ
Abstract Four novel peptides were isolated from the venoms of the solitary eumenine wasps Eumenes rubrofemoratus and Eumenes fraterculus. Their sequences were determined by MALDI-TOF/TOF (matrix assisted laser desorption/ionization time-of-flight mass spectrometry) analysis, Edman degradation and solid-phase synthesis. Two of them, eumenitin-R (LNLKGLIKKVASLLN) and eumenitin-F (LNLKGLFKKVASLLT), are highly homologous to eumenitin, an antimicrobial peptide from a solitary eumenine wasp, whereas the other two, EMP-ER (FDIMGLIKKVAGAL-NH(2)) and EMP-EF (FDVMGIIKKIAGAL-NH(2)), are similar to eumenine mastoparan-AF (EMP-AF), a mast cell degranulating peptide from a solitary eumenine wasp. These sequences have the characteristic features of linear cationic cytolytic peptides; rich in hydrophobic and basic amino acids with no disulfide bond, and accordingly, they can be predicted to adopt an amphipathic alpha-helix secondary structure. in fact, the CD (circular dichroism) spectra of these peptides showed significant alpha-helical conformation content in the presence of TFE (trifluoroethanol), SDS (sodium dodecylsulfate) and asolectin vesicles. in the biological evaluation, all the peptides exhibited a significant broad-spectrum antimicrobial activity, and moderate mast cell degranulation and leishmanicidal activities, but showed virtually no hemolytic activity. (C) 2011 Elsevier B.V. All rights reserved.
Keywords Solitary wasp
Linear cationic alpha-helical peptide
Amphipathic alpha-helix structure
Antimicrobial activity
Language English
Sponsor Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Grant number FAPESP: 2008/00173-4
CNPq: 307457/2008-7
CNPq: 477507/2008-5
Date 2011-06-01
Published in Toxicon. Oxford: Pergamon-Elsevier B.V., v. 57, n. 7-8, p. 1081-1092, 2011.
ISSN 0041-0101 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 1081-1092
Origin http://dx.doi.org/10.1016/j.toxicon.2011.04.014
Access rights Open access Open Access
Type Article
Web of Science ID WOS:000291833400017
URI http://repositorio.unifesp.br/handle/11600/33720

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