title: Penetratin-induced aggregation and subsequent dissociation of negatively charged phospholipid vesicles.
abstract: The interaction of the cellular delivery vector penetratin with a model system consisting of negatively charged phospholipid vesicles has been studied. Above a certain peptide to lipid molar ratio, the cationic oligopeptide induces vesicle aggregation. Interestingly, the aggregation is followed by spontaneous disaggregation, which may be related to membrane translocation of the peptide. Circular dichroism (CD) measurements indicate a conformational transition, from alpha-helix to antiparallel beta-pleated sheet, which is simultaneous with the aggregation process. The potential influence of spectroscopic artifacts on CD data due to the drastically increased turbidity during aggregation is discussed.
authors.affiliation: Department of Physical Chemistry, Chalmers University of Technology, SE-412 96 Gothenburg, Sweden. danielp@phc.chalmers.se
authors.forename: D
authors.initials: D
authors.lastname: Persson
authors.forename: P E
authors.initials: PE
authors.lastname: Thorén
authors.forename: B
authors.initials: B
authors.lastname: Nordén
mesh_terms: D002352:Carrier Proteins / Q000737:chemistry*; D002462:Cell Membrane / Q000378:metabolism; D057846:Cell-Penetrating Peptides; D002942:Circular Dichroism; D007700:Kinetics; D008956:Models, Chemical; D010455:Peptides / Q000737:chemistry; D010743:Phospholipids / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D021381:Protein Transport; D013053:Spectrophotometry; D013997:Time Factors
chemical_list: D002352:Carrier Proteins; D057846:Cell-Penetrating Peptides; D010455:Peptides; D010743:Phospholipids; C414409:penetratin