Chemical and biological characterization of four new linear cationic α-helical peptides from the venoms of two solitary eumenine wasps
Carregando...
Fontes externas
Fontes externas
Data
Orientador
Coorientador
Pós-graduação
Curso de graduação
Título da Revista
ISSN da Revista
Título de Volume
Editor
Elsevier
Tipo
Artigo
Direito de acesso
Acesso aberto
Fontes externas
Fontes externas
Resumo
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.
Descrição
Palavras-chave
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
Idioma
Inglês
Citação
Toxicon, v. 57, n. 7-8, p. 1081-1092, 2011.
