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Article Dans Une Revue PLoS ONE Année : 2008

The Homeodomain Derived Peptide Penetratin Induces Curvature of Fluid Membrane Domains

Résumé

Background : Protein membrane transduction domains that are able to cross the plasma membrane are present in several transcription factors, such as the homeodomain proteins and the viral proteins such as Tat of HIV-1. Their discovery resulted in both new concepts on the cell communication during development, and the conception of cell penetrating peptide vectors for internalisation of active molecules into cells. A promising cell penetrating peptide is Penetratin, which crosses the cell membranes by a receptor and metabolic energy-independent mechanism. Recent works have claimed that Penetratin and similar peptides are internalized by endocytosis, but other endocytosis-independent mechanisms have been proposed. Endosomes or plasma membranes crossing mechanisms are not well understood. Previously, we have shown that basic peptides induce membrane invaginations suggesting a new mechanism for uptake, ''physical endocytosis''.
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hal-02486911 , version 1 (21-02-2020)

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  • HAL Id : hal-02486911 , version 1

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Antonin Lamazière, Claude Wolf, Olivier Lambert, Gérard Chassaing, Germain Trugnan, et al.. The Homeodomain Derived Peptide Penetratin Induces Curvature of Fluid Membrane Domains. PLoS ONE, 2008. ⟨hal-02486911⟩
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