The antennapedia peptide penetratin translocates across lipid bilayers - the first direct observation.
The potential use of polypeptides and oligonucleotides for therapeutical purposes has been questioned because of their inherently poor cellular uptake. However, the 16-mer oligopeptide penetratin, derived from the homeodomain of Antennapedia, has been reported to enter cells readily via a non-endocytotic and receptor- and transporter-independent pathway, even when conjugated to large hydrophilic molecules. We here present the first study where penetratin is shown to traverse a pure lipid bilayer. The results support the idea that the uptake mechanism involves only the interaction of the peptide with the membrane lipids. Furthermore, we conclude that the translocation does not involve pore formation.
Thorén
P E
PE
Department of Physical Chemistry, Chalmers University of Technology, Gothenburg, Sweden.
Persson
D
D
Karlsson
M
M
Nordén
B
B
D000818:Animals; D051943:Antennapedia Homeodomain Protein; D002352:Carrier Proteins / Q000378:metabolism*; D057846:Cell-Penetrating Peptides; D004330:Drosophila / Q000378:metabolism; D029721:Drosophila Proteins; D018398:Homeodomain Proteins / Q000378:metabolism*; D008051:Lipid Bilayers / Q000378:metabolism*; D009687:Nuclear Proteins; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D021381:Protein Transport; D014157:Transcription Factors
D051943:Antennapedia Homeodomain Protein; C497974:Antp protein, Drosophila; D002352:Carrier Proteins; D057846:Cell-Penetrating Peptides; D029721:Drosophila Proteins; D018398:Homeodomain Proteins; D008051:Lipid Bilayers; D009687:Nuclear Proteins; D010446:Peptide Fragments; D014157:Transcription Factors; C414409:penetratin