NR AHPC
AU Lundberg,P.; Magzoub,M.; Lindberg,M.; Hällbrink,M.; Jarvet,J.; Eriksson,L.E.G.; Langel,U.; Gräslund,A.
TI Cell membrane translocation of the N-terminal (1-28) part of the prion protein
QU Biochemical and Biophysical Research Communications 2002 Nov 22; 299(1): 85-90
PT journal article
AB 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 (PrPsc) form of the protein and its amyloidic transformation.
AD Department of Neurochemistry and Neurotoxicology, Stockholm University, SE-106 91, Stockholm, Sweden
SP englisch
PO USA