Conformation and lytic activity of eumenine mastoparan: A new antimicrobial peptide from wasp venom

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorDos Santos Cabrera, M. P.
dc.creatorDe Souza, B. M.
dc.creatorFontana, R.
dc.creatorKonno, K.
dc.creatorPalma, Mario Sergio
dc.creatorDe Azevedo, W. F.
dc.creatorRuggiero Neto, J.
dc.date2014-05-27T11:21:08Z
dc.date2016-10-25T18:19:51Z
dc.date2014-05-27T11:21:08Z
dc.date2016-10-25T18:19:51Z
dc.date2004-09-01
dc.date.accessioned2017-04-06T01:10:09Z
dc.date.available2017-04-06T01:10:09Z
dc.identifierJournal of Peptide Research, v. 64, n. 3, p. 95-103, 2004.
dc.identifier1397-002X
dc.identifierhttp://hdl.handle.net/11449/67847
dc.identifierhttp://acervodigital.unesp.br/handle/11449/67847
dc.identifier10.1111/j.1399-3011.2004.00173.x
dc.identifierWOS:000223280800002
dc.identifier2-s2.0-4444323580
dc.identifierhttp://dx.doi.org/10.1111/j.1399-3011.2004.00173.x
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/889253
dc.descriptionEumenine mastoparan-AF (EMP-AF) is a novel membrane active tetradecapeptide recently isolated from the venom of solitary wasp, Anterhynchium flavomarginatum micado. It was reported previously that EMP-AF peptide presented low cytolytic activities in human erythrocytes and in RBL-2H3 mast cells. In the present work, we observed that this peptide is able to permeate anionic liposomes, and in less extension also the neutral ones. We present evidences showing that the permeation ability is well correlated with the amount of helical conformation assumed by the peptides in these environments. This peptide also showed a broad-spectrum inhibitory activity against Gram-positive and Gram-negative bacteria. The permeability of liposomes and the antibiotic effect showed a significant reduction when C-terminus was deamidated (in acidic form). The removal of the three first amino acid residues from the N-terminus rendered the peptide inactive both in liposomes and in bacteria. The results suggest that the mechanism of action involves a threshold in the accumulation of the peptide at level of cell membrane.
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.languageeng
dc.relationJournal of Peptide Research
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectAmphiphilic helix
dc.subjectAntimicrobial peptide
dc.subjectEumenine mastoparan
dc.subjectMembrane permeation
dc.subjectWasp venom
dc.subjectantiinfective agent
dc.subjecteumenine mastoparan AF
dc.subjectliposome
dc.subjectunclassified drug
dc.subjectwasp venom
dc.subjectamino terminal sequence
dc.subjectAnterhynchium flavomarginatum micado
dc.subjectantibacterial activity
dc.subjectantimicrobial activity
dc.subjectbacterial membrane
dc.subjectcarboxy terminal sequence
dc.subjectcell membrane permeability
dc.subjectcontrolled study
dc.subjectdeamination
dc.subjectdrug mechanism
dc.subjectGram negative bacterium
dc.subjectGram positive bacterium
dc.subjectnonhuman
dc.subjectpriority journal
dc.subjectprotein conformation
dc.subjectstructure activity relation
dc.subjectwasp
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectAnti-Bacterial Agents
dc.subjectCell Membrane Permeability
dc.subjectCircular Dichroism
dc.subjectHumans
dc.subjectInsect Proteins
dc.subjectLiposomes
dc.subjectMicrobial Sensitivity Tests
dc.subjectMolecular Sequence Data
dc.subjectProtein Conformation
dc.subjectWasp Venoms
dc.subjectWasps
dc.subjectBacteria (microorganisms)
dc.subjectMegascolia flavifrons
dc.subjectNegibacteria
dc.subjectPosibacteria
dc.subjectVespidae
dc.titleConformation and lytic activity of eumenine mastoparan: A new antimicrobial peptide from wasp venom
dc.typeOtro


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