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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state

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Alvares, Dayane S. ; Wilke, Natalia ; Ruggiero Neto, Joao ; Fanani, Maria Laura
Total Authors: 4
Document type: Journal article
Source: Chemistry and Physics of Lipids; v. 207, n. A, p. 38-48, OCT 2017.
Web of Science Citations: 8

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 MPl-lipid membrane interaction was studied using Langmuir phosphatidylcholine and phosphatidylseririe (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. (AU)

FAPESP's process: 11/51684-1 - System biology as experimental strategy for discovery of novel natural products in the fauna of venomous arthropods from São Paulo State
Grantee:Mario Sergio Palma
Support type: BIOTA-FAPESP Program - Thematic Grants
FAPESP's process: 12/08147-8 - Study of domains formation in model membranes induced by antimicrobial peptides and their action interfacial
Grantee:Dayane dos Santos Alvares
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 11/11640-5 - Interaction of lytic peptides and model membranes: intefacial action and induction of lipid domains
Grantee:João Ruggiero Neto
Support type: Regular Research Grants
FAPESP's process: 15/25619-9 - Effect of aminophospholipids and of the pH on the interfacial activity of the anticancer peptide Polybia-MP1 and analogs in model membranes
Grantee:João Ruggiero Neto
Support type: Regular Research Grants
FAPESP's process: 15/01508-3 - Interaction of the antimicrobial and antitumor peptide, Polybia-MP1, with lipid-domains
Grantee:Dayane dos Santos Alvares
Support type: Scholarships abroad - Research Internship - Doctorate
FAPESP's process: 15/25620-7 - Interaction membrane/peptide: mechanical and electrostatic properties in system with lipid domains
Grantee:Dayane dos Santos Alvares
Support type: Scholarships in Brazil - Post-Doctorate