Lipid domain separation, bilayer thickening and pearling induced by the cell penetrating peptide penetratin
Résumé
Protein membrane transduction domains are able to translocate through cell membranes. This capacity resulted in new concepts on cell communication and in the design of vectors for internalization of active molecules into cells. Penetratin crosses the plasma membrane by a receptor and metabolic energy-independent mechanism which is at present unknown. A better knowledge of its interaction with phospholipids will help to understand the molecular mechanisms of cell penetration. Here, we investigated the role of lipid composition on penetratin induced membrane perturbations by X-ray diffraction, microscopy and 31 P-NMR. Penetratin showed the ability to induce phospholipid domain separation, membrane bilayer thickening, formation of vesicles, membrane undulations and tubular pearling. These data demonstrate its capacity to increase membrane curvature and suggest that dynamic phospholipid-penetratin complexes can be organized in different structural arrangements. These properties and their implications in peptide membrane translocation capacity are discussed.
Mots clés
Lipid phase separation
Membrane curvature
Membrane pearling
Membrane thickening
Penetratin
Physical endocytosis 2 Abbreviations Chol
cholesterol
CPP
cell penetrating peptide
GUV
giant unilamellar vesicle
LUV
Large unilamellar vesicle
MLV
multilamellar vesicle
PC
L-α-Phosphatidylcholine
PE
L-α- Phosphatidyl-ethanolamine
PG
L-α-Phosphatidyl-DL-glycerol
R9
nona-arginine peptide
SAXS
small angle X-ray scattering
SM
Sphingomyeline
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