The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.chemphyslip.2017.08.001 http://hdl.handle.net/11449/175046 |
Resumo: | 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. |
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The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase stateAntimicrobial peptideBrewster angle microscopyLipid domainsMembrane penetrationPeptide adsorptionPolybia-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.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Agencia Nacional de Promoción Científica y TecnológicaCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Consejo Nacional de Investigaciones Científicas y TécnicasUNESP – São Paulo State University IBILCE Department of PhysicsCentro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC-CONICET) Departamento de Química Biológica Facultas de Ciencias Químicas Universidad Nacional de CórdobaUNESP – São Paulo State University IBILCE Department of PhysicsFAPESP: 2011/11640-5FAPESP: 2011/51684-1FAPESP: 2012/08147-8FAPESP: 2015/01508-3FAPESP: 2015/25619-9FAPESP: 2015/25620-7Agencia Nacional de Promoción Científica y Tecnológica: PICT 2012-0344Agencia Nacional de Promoción Científica y Tecnológica: PICT 2014-1627Consejo Nacional de Investigaciones Científicas y Técnicas: PIP 2013-2015Universidade Estadual Paulista (Unesp)Universidad Nacional de CórdobaAlvares, Dayane S. [UNESP]Wilke, NataliaRuggiero Neto, João [UNESP]Fanani, Maria Laura2018-12-11T17:13:58Z2018-12-11T17:13:58Z2017-10-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article38-48application/pdfhttp://dx.doi.org/10.1016/j.chemphyslip.2017.08.001Chemistry and Physics of Lipids, v. 207, p. 38-48.1873-29410009-3084http://hdl.handle.net/11449/17504610.1016/j.chemphyslip.2017.08.0012-s2.0-850274151022-s2.0-85027415102.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengChemistry and Physics of Lipids1,220info:eu-repo/semantics/openAccess2023-10-04T06:08:44Zoai:repositorio.unesp.br:11449/175046Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462023-10-04T06:08:44Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state |
title |
The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state |
spellingShingle |
The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state Alvares, Dayane S. [UNESP] Antimicrobial peptide Brewster angle microscopy Lipid domains Membrane penetration Peptide adsorption |
title_short |
The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state |
title_full |
The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state |
title_fullStr |
The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state |
title_full_unstemmed |
The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state |
title_sort |
The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state |
author |
Alvares, Dayane S. [UNESP] |
author_facet |
Alvares, Dayane S. [UNESP] Wilke, Natalia Ruggiero Neto, João [UNESP] Fanani, Maria Laura |
author_role |
author |
author2 |
Wilke, Natalia Ruggiero Neto, João [UNESP] Fanani, Maria Laura |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Universidad Nacional de Córdoba |
dc.contributor.author.fl_str_mv |
Alvares, Dayane S. [UNESP] Wilke, Natalia Ruggiero Neto, João [UNESP] Fanani, Maria Laura |
dc.subject.por.fl_str_mv |
Antimicrobial peptide Brewster angle microscopy Lipid domains Membrane penetration Peptide adsorption |
topic |
Antimicrobial peptide Brewster angle microscopy Lipid domains Membrane penetration Peptide adsorption |
description |
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. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-10-01 2018-12-11T17:13:58Z 2018-12-11T17:13:58Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.chemphyslip.2017.08.001 Chemistry and Physics of Lipids, v. 207, p. 38-48. 1873-2941 0009-3084 http://hdl.handle.net/11449/175046 10.1016/j.chemphyslip.2017.08.001 2-s2.0-85027415102 2-s2.0-85027415102.pdf |
url |
http://dx.doi.org/10.1016/j.chemphyslip.2017.08.001 http://hdl.handle.net/11449/175046 |
identifier_str_mv |
Chemistry and Physics of Lipids, v. 207, p. 38-48. 1873-2941 0009-3084 10.1016/j.chemphyslip.2017.08.001 2-s2.0-85027415102 2-s2.0-85027415102.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Chemistry and Physics of Lipids 1,220 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
38-48 application/pdf |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
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1799964435271385088 |