Cell membrane translocation of the N-terminal (1-28) part of the prion protein
2002 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 299, no 1, 85-90 p.Article in journal (Refereed) Published
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 P-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 arnyloidic transformation.
Place, publisher, year, edition, pages
2002. Vol. 299, no 1, 85-90 p.
prion protein N-terminus, cell penetrating peptide, aggregation, beta-structure, membrane interaction
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:su:diva-23351DOI: 10.1016/S0006-291X(02)02595-0ISI: 000179496700013OAI: oai:DiVA.org:su-23351DiVA: diva2:191479