Article Dans Une Revue Scientific Reports Année : 2017

Cargo self-assembly rescues affinity of cell-penetrating peptides to lipid membranes

Vivien Walter
Tatiana Schmatko
Pierre Muller
André Pierre Schroder
Ashutosh Chilkoti
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Carlos Marques

Résumé

Although cationic cell-penetrating peptides (CPPs) are able to bind to cell membranes, thus promoting cell internalization by active pathways, attachment of cargo molecules to CPPs invariably reduces their cellular uptake. We show here that CPP binding to lipid bilayers, a simple model of the cell membrane, can be recovered by designing cargo molecules that self-assemble into spherical micelles and increase the local interfacial density of CPP on the surface of the cargo. Experiments performed on model giant unilamellar vesicles under a confocal laser scanning microscope show that a family of thermally responsive elastin-like polypeptides that exhibit temperature-triggered micellization can promote temperature triggered attachment of the micelles to membranes, thus rescuing by self-assembly the cargo-induced loss of the CPP affinity to bio-membranes.

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hal-02324921 , version 1 (31-07-2024)

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Andreas Weinberger, Vivien Walter, Sarah Macewan, Tatiana Schmatko, Pierre Muller, et al.. Cargo self-assembly rescues affinity of cell-penetrating peptides to lipid membranes. Scientific Reports, 2017, 7 (1), pp.43963. ⟨10.1038/srep43963⟩. ⟨hal-02324921⟩
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