New Insight into the Mechanism of Action of Wasp Mastoparan Peptides: Lytic Activity and Clustering Observed with Giant Vesicles

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dc.contributor.authordos Santos Cabrera, Marcia P. [UNESP]
dc.contributor.authorAlvares, Dayane S. [UNESP]
dc.contributor.authorLeite, Natalia B. [UNESP]
dc.contributor.authorde Souza, Bibiana Monson [UNESP]
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.contributor.authorRiske, Karin A.
dc.contributor.authorNeto, Joao Ruggiero [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2014-05-20T14:02:36Z
dc.date.available2014-05-20T14:02:36Z
dc.date.issued2011-09-06
dc.description.abstractAntimicrobial peptides of the mastoparans family exert their bactericidal activity by binding to lipid membranes, inducing pores or defects and leaking the internal contents of vesicles and cells. However, this does not seem to be the only mechanism at play, and they might be important in the search for improved peptides with lower undesirable side effects. This work deals with three mastoparans peptides, Polybia-MP-1(MP-1), N2-Polybia-MP-1 (N-MP-1), and Mastoparan X (MPX), which exhibit high sequence homology. They all have three lysine residues and amidated C termini, but because of the presence of two, one, and no aspartic acid residues, respectively, they have +2, +3, and +4 net charges at physiological pH. Here we focus on the effects of these mastoparans peptides on anionic model membranes made of palmitoleyoilphosphatidylcholine (POPC) and palmitoleyoilphosphatidylglycerol (POPG) at 1:1 and 3:1 molar ratios in the presence and in the absence of saline buffer. Zeta potential experiments were carried out to measure the extent of the peptides' binding and accumulation at the vesicle surface, and CD spectra were acquired to quantify the helical structuring of the peptides upon binding. Giant unilamellar vesicles were observed under phase contrast and fluorescence microscopy. We found that the three peptides induced the leakage of GUVs at a gradual rate with many characteristics of the graded mode. This process was faster in the absence of saline buffer. Additionally, we observed that the peptides induced the formation of dense regions of phospholipids and peptides on the GUV surface. This phenomenon was easily observable for the more charged peptides.(MPX > N-MP-1 > MP-1) and in the absence of added salt. Our data suggest that these mastoparans accumulate on the bilayer surface and induce a transient interruption to its barrier properties, leaking the vesicle contents. Next, the bilayer recovers its continuity, but this happens in an inhomogeneous way, forming a kind of ply with peptides sandwiched between two juxtaposed membranes. Eventually, a peptide-lipid aggregate forming a lump is formed at high peptide-to-lipid ratios.en
dc.description.affiliationUNESP São Paulo State Univ, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUNESP São Paulo State Univ, Ctr Studies Social Insects, Inst Biosci, BR-13506900 Rio Claro, SP, Brazil
dc.description.affiliationUNIFESP Univ Fed São Paulo, Dept Biofis, BR-0403932 São Paulo, Brazil
dc.description.affiliationUnespUNESP São Paulo State Univ, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespUNESP São Paulo State Univ, Ctr Studies Social Insects, Inst Biosci, BR-13506900 Rio Claro, SP, Brazil
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipIdCNPq: 477507/2008-5
dc.description.sponsorshipIdFAPESP: 10/11823-0
dc.description.sponsorshipIdFAPESP: 06/57122-7
dc.description.sponsorshipIdFAPESP: 07/03657-0
dc.format.extent10805-10813
dc.identifierhttp://dx.doi.org/10.1021/la202608r
dc.identifier.citationLangmuir. Washington: Amer Chemical Soc, v. 27, n. 17, p. 10805-10813, 2011.
dc.identifier.doi10.1021/la202608r
dc.identifier.issn0743-7463
dc.identifier.lattes2901888624506535
dc.identifier.urihttp://hdl.handle.net/11449/22067
dc.identifier.wosWOS:000294373300059
dc.language.isoeng
dc.publisherAmer Chemical Soc
dc.relation.ispartofLangmuir
dc.relation.ispartofjcr3.789
dc.relation.ispartofsjr1,479
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.titleNew Insight into the Mechanism of Action of Wasp Mastoparan Peptides: Lytic Activity and Clustering Observed with Giant Vesiclesen
dc.typeArtigo
dcterms.licensehttp://pubs.acs.org/page/copyright/index.html
dcterms.rightsHolderAmer Chemical Soc
unesp.author.lattes2901888624506535
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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Artigos - Física - IBILCE
Rio Claro - CEIS - Centro de Estudos de Insetos Sociais