Abstract

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 (67 kDa) into several cell lines. The (1–28) peptide has a strong tendency for aggregation and β-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 β-structure may be relevant as a seed for the conversion into the scrapie (PrP Sc) form of the protein and its amyloidic transformation.

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