The interfacial properties of the peptide Polybia-MP1 and its interaction with DPPC are modulated by lateral electrostatic attractions

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dc.contributor.authorAlvares, Dayane S. [UNESP]
dc.contributor.authorFanani, Maria Laura
dc.contributor.authorRuggiero Neto, João [UNESP]
dc.contributor.authorWilke, Natalia
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Nacional de Córdoba
dc.date.accessioned2018-12-11T16:59:32Z
dc.date.available2018-12-11T16:59:32Z
dc.date.issued2016-02-01
dc.description.abstractPolybia-MP1 (IDWKKLLDAAKQIL-NH2), extracted from the Brazilian wasp Polybia paulista, exhibits a broad-spectrum bactericidal activity without being hemolytic and cytotoxic. In the present study, we analyzed the surface properties of the peptide and its interaction with DPPC in Langmuir monolayers. Polybia-MP1 formed stable monolayers, with lateral areas and surface potential values suggesting a mostly α-helical structure oriented near perpendicular to the membrane plane. In DPPC-peptide mixed monolayers, MP1 co-crystallized with the lipid forming branched domains only when the subphase was pure water. On subphases with high salt concentrations or at acidic or basic conditions, the peptide formed less densely packed films and was excluded from the domains, indicating the presence of attractive electrostatic interactions between peptides, which allow them to get closer to each other and to interact with DPPC probably as a consequence of a particular peptide arrangement. The residues responsible of the peptide-peptide attraction are suggested to be the anionic aspartic acids and the cationic lysines, which form a salt bridge, leading to oriented interactions in the crystal and thereby to branched domains. For this peptide, the balance between total attractive and repulsive interactions may be finely tuned by the aqueous ionic strength and pH, and since this effect is related with lysines and aspartic acids, similar effects may also occur in other peptides containing these residues in their sequences.en
dc.description.affiliationUNESP - São Paulo State University IBILCE Department of Physics
dc.description.affiliationCentro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC-CONICET) Departamento de Química Biológica Facultas de Ciencias Químicas Universidade Nacional de Córdoba
dc.description.affiliationUnespUNESP - São Paulo State University IBILCE Department of Physics
dc.format.extent393-402
dc.identifierhttp://dx.doi.org/10.1016/j.bbamem.2015.12.010
dc.identifier.citationBiochimica et Biophysica Acta - Biomembranes, v. 1858, n. 2, p. 393-402, 2016.
dc.identifier.doi10.1016/j.bbamem.2015.12.010
dc.identifier.issn1879-2642
dc.identifier.issn0005-2736
dc.identifier.scopus2-s2.0-84949595510
dc.identifier.urihttp://hdl.handle.net/11449/172288
dc.language.isoeng
dc.relation.ispartofBiochimica et Biophysica Acta - Biomembranes
dc.relation.ispartofsjr1,495
dc.rights.accessRightsAcesso restrito
dc.sourceScopus
dc.subjectDomain shape
dc.subjectLangmuir-monolayer
dc.subjectLipid-peptide co-crystals
dc.subjectMembrane electrostatic interactions
dc.subjectPeptide-peptide lateral interactions
dc.titleThe interfacial properties of the peptide Polybia-MP1 and its interaction with DPPC are modulated by lateral electrostatic attractionsen
dc.typeArtigo

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