title: Distinct behaviour of the homeodomain derived cell penetrating peptide penetratin in interaction with different phospholipids.
abstract: BACKGROUND
  Penetratin is a protein transduction domain derived from the homeoprotein Antennapedia. Thereby it is currently used as a cell penetrating peptide to introduce diverse molecules into eukaryotic cells, and it could also be involved in the cellular export of transcription factors. Moreover, it has been shown that it is able to act as an antimicrobial agent. The mechanisms involved in all these processes are quite controversial.
  
  
  RESULTS
  In this article, we report spectroscopic, calorimetric and biochemical data on the penetratin interaction with three different phospholipids: phosphatidylcholine (PC) and phosphatidylethanolamine (PE) to mimic respectively the outer and the inner leaflets of the eukaryotic plasma membrane and phosphatidylglycerol (PG) to mimic the bacterial membrane. We demonstrate that with PC, penetratin is able to form vesicle aggregates with no major change in membrane fluidity and presents no well defined secondary structure organization. With PE, penetratin aggregates vesicles, increases membrane rigidity and acquires an α-helical structure. With PG membranes, penetratin does not aggregate vesicles but decreases membrane fluidity and acquires a structure with both α-helical and β-sheet contributions.
  
  
  CONCLUSIONS
  These data from membrane models suggest that the different penetratin actions in eukaryotic cells (membrane translocation during export and import) and on prokaryotes may result from different peptide and lipid structural arrangements. The data suggest that, for eukaryotic cell penetration, penetratin does not acquire classical secondary structure but requires a different conformation compared to that in solution.
authors.affiliation: CNRS, UMR 7203, Laboratoire des Biomolécules, Groupe N. J. Conté, Paris, France.
authors.forename: Ofelia
authors.initials: O
authors.lastname: Maniti
authors.forename: Isabel
authors.initials: I
authors.lastname: Alves
authors.forename: Germain
authors.initials: G
authors.lastname: Trugnan
authors.forename: Jesus
authors.initials: J
authors.lastname: Ayala-Sanmartin
mesh_terms: D051943:Antennapedia Homeodomain Protein / Q000737:chemistry; D002152:Calorimetry, Differential Scanning / Q000379:methods; D002352:Carrier Proteins / Q000737:chemistry*; D002462:Cell Membrane / Q000378:metabolism; D057846:Cell-Penetrating Peptides; D008051:Lipid Bilayers / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D010713:Phosphatidylcholines / Q000737:chemistry; D010714:Phosphatidylethanolamines / Q000737:chemistry; D010715:Phosphatidylglycerols / Q000737:chemistry; D010743:Phospholipids / Q000737:chemistry*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013053:Spectrophotometry
chemical_list: D051943:Antennapedia Homeodomain Protein; D002352:Carrier Proteins; D057846:Cell-Penetrating Peptides; D008051:Lipid Bilayers; D010455:Peptides; D010713:Phosphatidylcholines; D010714:Phosphatidylethanolamines; D010715:Phosphatidylglycerols; D010743:Phospholipids; C483858:phosphatidylethanolamine; C414409:penetratin