dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorRangel, Marisa
dc.creatordos Santos Cabrera, Marcia Perez
dc.creatorKazuma, Kohei
dc.creatorAndo, Kenji
dc.creatorWang, Xiaoyu
dc.creatorKato, Manabu
dc.creatorNihei, Ken-ichi
dc.creatorHirata, Izaura Yoshico
dc.creatorCross, Tyra J.
dc.creatorGarcia, Angélica Nunes
dc.creatorFaquim-Mauro, Eliana L.
dc.creatorFranzolin, Marcia Regina
dc.creatorFuchino, Hiroyuki
dc.creatorMori-Yasumoto, Kanami
dc.creatorSekita, Setsuko
dc.creatorKadowaki, Makoto
dc.creatorSatake, Motoyoshi
dc.creatorKonno, Katsuhiro
dc.date2014-05-27T11:25:54Z
dc.date2016-10-25T18:34:00Z
dc.date2014-05-27T11:25:54Z
dc.date2016-10-25T18:34:00Z
dc.date2011-06-01
dc.date.accessioned2017-04-06T01:50:44Z
dc.date.available2017-04-06T01:50:44Z
dc.identifierToxicon, v. 57, n. 7-8, p. 1081-1092, 2011.
dc.identifier0041-0101
dc.identifier1879-3150
dc.identifierhttp://hdl.handle.net/11449/72463
dc.identifierhttp://acervodigital.unesp.br/handle/11449/72463
dc.identifier10.1016/j.toxicon.2011.04.014
dc.identifier2-s2.0-79956338547.pdf
dc.identifier2-s2.0-79956338547
dc.identifierhttp://dx.doi.org/10.1016/j.toxicon.2011.04.014
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/893331
dc.descriptionFour 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.
dc.languageeng
dc.relationToxicon
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectAmphipathic α-helix structure
dc.subjectAntimicrobial activity
dc.subjectLinear cationic α-helical peptide
dc.subjectSolitary wasp
dc.subjectamino acid
dc.subjectantimicrobial cationic peptide
dc.subjectazolectin
dc.subjectdodecyl sulfate sodium
dc.subjecteumeninine mastoparan AF
dc.subjecteumeninine mastoparan EF
dc.subjecteumeninine mastoparan ER
dc.subjecteumenitin F
dc.subjecteumenitin R
dc.subjectinsect venom
dc.subjectmast cell degranulating peptide
dc.subjecttrifluoroethanol
dc.subjectunclassified drug
dc.subjectalpha helix
dc.subjectanimal cell
dc.subjectantimicrobial activity
dc.subjectantiprotozoal activity
dc.subjectcircular dichroism
dc.subjectconcentration response
dc.subjectcontrolled study
dc.subjectdrug screening
dc.subjectEumenes fraterculus
dc.subjectEumenes rubrofemoratus
dc.subjectfemale
dc.subjecthemolysis
dc.subjecthydrophobicity
dc.subjectmast cell degranulation
dc.subjectmatrix assisted laser desorption ionization time of flight mass spectrometry
dc.subjectmouse
dc.subjectnonhuman
dc.subjectpeptide analysis
dc.subjectpriority journal
dc.subjectprotein secondary structure
dc.subjectsequence analysis
dc.subjectsequence homology
dc.subjectsolid phase synthesis
dc.subjectstructure analysis
dc.subjectwasp
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectAnti-Bacterial Agents
dc.subjectCations
dc.subjectCircular Dichroism
dc.subjectMass Spectrometry
dc.subjectMolecular Sequence Data
dc.subjectPeptides
dc.subjectProtein Structure, Secondary
dc.subjectVenoms
dc.subjectWasps
dc.subjectEumenes
dc.subjectMegascolia flavifrons
dc.titleChemical and biological characterization of four new linear cationic α-helical peptides from the venoms of two solitary eumenine wasps
dc.typeOtro


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