Lipid domain separation, bilayer thickening and pearling induced by the cell penetrating peptide penetratin.
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.
Lamazière
Antonin
A
Laboratoire des BioMolécules, Groupe N. J. Conté, Paris, France.
Maniti
Ofelia
O
Wolf
Claude
C
Lambert
Olivier
O
Chassaing
Gérard
G
Trugnan
Germain
G
Ayala-Sanmartin
Jesus
J
D002352:Carrier Proteins / Q000737:chemistry*; D057846:Cell-Penetrating Peptides / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D008563:Membrane Lipids / Q000737:chemistry*
D002352:Carrier Proteins; D057846:Cell-Penetrating Peptides; D008051:Lipid Bilayers; D008563:Membrane Lipids; C414409:penetratin