Cell membrane translocation of the N-terminal (1-28) part of the prion protein.
The N-terminal (1-28) part of the mouse prion protein (PrP) is a cell penetrating peptide, capable of transporting large hydrophilic cargoes through a cell membrane. Confocal fluorescence microscopy shows that it transports the protein avidin (67kDa) into several cell lines. The (1-28) peptide has a strong tendency for aggregation and beta-structure formation, particularly in interaction with negatively charged phospholipid membranes. The findings have implications for how prion proteins with uncleaved signal peptides in the N-termini may enter into cells, which is important for infection. The secondary structure conversion into beta-structure may be relevant as a seed for the conversion into the scrapie (PrP(Sc)) form of the protein and its amyloidic transformation.
Lundberg
P
P
Department of Neurochemistry and Neurotoxicology, Stockholm University, SE-106 91, Stockholm, Sweden.
Magzoub
M
M
Lindberg
M
M
Hällbrink
M
M
Jarvet
J
J
Eriksson
L E G
LE
Langel
U
U
Gräslund
A
A
D000595:Amino Acid Sequence; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D002942:Circular Dichroism; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D018613:Microscopy, Confocal; D008969:Molecular Sequence Data; D010452:Peptide Biosynthesis; D010455:Peptides / Q000737:chemistry; D018620:PrPSc Proteins / Q000378:metabolism; D011328:Prions / Q000737:chemistry* / Q000378:metabolism*; D021382:Protein Sorting Signals; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D013997:Time Factors; D014407:Tumor Cells, Cultured
D010455:Peptides; D018620:PrPSc Proteins; D011328:Prions; D021382:Protein Sorting Signals