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

• Autor(a) principal: Rangel, Marisa
• Data de Publicação: 2011
• Outros Autores: dos Santos Cabrera, Marcia Perez [UNESP], Kazuma, Kohei, Ando, Kenji, Wang, Xiaoyu, Kato, Manabu, Nihei, Ken-ichi, Hirata, Izaura Yoshico, Cross, Tyra J., Garcia, Angélica Nunes, Faquim-Mauro, Eliana L., Franzolin, Marcia Regina, Fuchino, Hiroyuki, Mori-Yasumoto, Kanami, Sekita, Setsuko, Kadowaki, Makoto, Satake, Motoyoshi, Konno, Katsuhiro
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UNESP
• Texto Completo: http://dx.doi.org/10.1016/j.toxicon.2011.04.014; http://hdl.handle.net/11449/72463
• topic: Amphipathic α-helix structure; Antimicrobial activity; Linear cationic α-helical peptide; Solitary wasp; amino acid; antimicrobial cationic peptide; azolectin; dodecyl sulfate sodium; eumeninine mastoparan AF; eumeninine mastoparan EF; eumeninine mastoparan ER; eumenitin F; eumenitin R; insect venom; mast cell degranulating peptide; trifluoroethanol; unclassified drug; alpha helix; animal cell; antimicrobial activity; antiprotozoal activity; circular dichroism; concentration response; controlled study; drug screening; Eumenes fraterculus; Eumenes rubrofemoratus; female; hemolysis; hydrophobicity; mast cell degranulation; matrix assisted laser desorption ionization time of flight mass spectrometry; mouse; nonhuman; peptide analysis; priority journal; protein secondary structure; sequence analysis; sequence homology; solid phase synthesis; structure analysis; wasp; Amino Acid Sequence; Animals; Anti-Bacterial Agents; Cations; Circular Dichroism; Mass Spectrometry; Molecular Sequence Data; Peptides; Protein Structure, Secondary; Venoms; Wasps; Eumenes; Megascolia flavifrons

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 α-helix secondary structure. In fact, the CD (circular dichroism) spectra of these peptides showed significant α-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. © 2011 Elsevier Ltd.