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dc.contributor.author Alvares, Dayane S.
dc.contributor.author Fanani, Maria Laura
dc.contributor.author Ruggiero Neto, João
dc.contributor.author Wilke, Natalia
dc.date.available 2018-07-02T20:32:22Z
dc.date.issued 2016-02
dc.identifier.citation Alvares, Dayane S.; Fanani, Maria Laura; Ruggiero Neto, João; Wilke, Natalia; The interfacial properties of the peptide Polybia-MP1 and its interaction with DPPC are modulated by lateral electrostatic attractions; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1858; 2; 2-2016; 393-402
dc.identifier.issn 0005-2736
dc.identifier.uri http://hdl.handle.net/11336/50946
dc.description.abstract Polybia-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.
dc.format application/pdf
dc.language.iso eng
dc.publisher Elsevier Science
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject DOMAIN SHAPE
dc.subject LANGMUIR-MONOLAYER
dc.subject LIPID-PEPTIDE CO-CRYSTALS
dc.subject MEMBRANE ELECTROSTATIC INTERACTIONS
dc.subject PEPTIDE-PEPTIDE LATERAL INTERACTIONS
dc.subject.classification Otras Ciencias Biológicas
dc.subject.classification Ciencias Biológicas
dc.subject.classification CIENCIAS NATURALES Y EXACTAS
dc.title The interfacial properties of the peptide Polybia-MP1 and its interaction with DPPC are modulated by lateral electrostatic attractions
dc.type info:eu-repo/semantics/article
dc.type info:ar-repo/semantics/artículo
dc.type info:eu-repo/semantics/publishedVersion
dc.date.updated 2018-06-29T16:45:41Z
dc.journal.volume 1858
dc.journal.number 2
dc.journal.pagination 393-402
dc.journal.pais Países Bajos
dc.journal.ciudad Amsterdam
dc.description.fil Fil: Alvares, Dayane S.. Universidade Estadual Paulista Julio de Mesquita Filho; Brasil
dc.description.fil Fil: Fanani, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
dc.description.fil Fil: Ruggiero Neto, João. Universidade Estadual Paulista Julio de Mesquita Filho; Brasil
dc.description.fil Fil: Wilke, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
dc.journal.title Biochimica et Biophysica Acta - Biomembranes
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbamem.2015.12.010
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273615004083
dc.conicet.fuente individual


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info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Atribución-NoComercial-SinDerivadas 2.5 Argentina (CC BY-NC-ND 2.5 AR)