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dc.contributor.author
Alvares, Dayane S.
dc.contributor.author
Wilke, Natalia
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dc.contributor.author
Ruggiero Neto, João
dc.contributor.author
Fanani, Maria Laura
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dc.date.available
2018-08-29T17:27:25Z
dc.date.issued
2017-10
dc.identifier.citation
Alvares, Dayane S.; Wilke, Natalia; Ruggiero Neto, João; Fanani, Maria Laura; The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state; Elsevier Ireland; Chemistry And Physics Of Lipids; 207; 10-2017; 38-48
dc.identifier.issn
0009-3084
dc.identifier.uri
http://hdl.handle.net/11336/57518
dc.description.abstract
Polybia-MP1 or simply MP1 (IDWKKLLDAAKQIL-NH2) is a peptide with broad-spectrum bactericidal activity and a strong inhibitory effect against cancer cells. The aim of this work was to evaluate the effect of biophysical properties such as membrane texture and film thickness on MP1 interaction with neutral and anionic lipid membranes. For this purpose, we first explored the peptide's surface behavior. MP1 showed high surface activity, adsorbing onto bare air/aqueous interfaces up to higher surface pressures than the collapse pressure of MP1 Langmuir films. The MP1-lipid membrane interaction was studied using Langmuir phosphatidylcholine and phosphatidylserine (PS) monolayers as model membrane systems. PS was chosen since this negatively charged lipid was found predominantly on the outer leaflet of tumor cells, and it enhances MP1 activity for PS-containing membranes to a greater extent than for other negatively charged lipids. MP1 incorporated into anionic PS monolayers, which show a liquid-expanded (LE) phase or LE-liquid-condensed (LC) phase coexistence, up to lipid-packing densities higher than those of cell membranes. The mixed lipid/MP1 films were explored by Brewster angle microscopy and atomic force microscopy. MP1 partitioned preferentially into the LE phase state of PS films, and were thus excluded from the coexisting LC phase. This interaction had strong electrostatic bases: in pure water, the lipid-peptide interaction was strong enough to induce formation of reversible lipid-peptide 3D structures associated with the interface. MP1 incorporation into the LE phase was accompanied by a shift of the phase transition pressure to higher values and a thinning of the lipid film. These results showed a clear correlation between peptide penetration capacity and the presence or induction of the thin LE phase. This capacity to regulate membrane physical properties may be of relevance in the binding, incorporation and membrane selectivity of this promising antitumor peptide.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Ireland
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights
Atribución-NoComercial-CompartirIgual 2.5 Argentina (CC BY-NC-SA 2.5 AR)
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Antimicrobial Peptide
dc.subject
Brewster Angle Microscopy
dc.subject
Lipid Domains
dc.subject
Membrane Penetration
dc.subject
Peptide Adsorption
dc.subject.classification
Otras Ciencias Biológicas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-08-27T18:58:07Z
dc.journal.volume
207
dc.journal.pagination
38-48
dc.journal.pais
Irlanda
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dc.description.fil
Fil: Alvares, Dayane S.. Universidade de Sao Paulo; 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.description.fil
Fil: Ruggiero Neto, João. Universidade de Sao Paulo; 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.journal.title
Chemistry And Physics Of Lipids
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pubmed/28802697
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.chemphyslip.2017.08.001
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