Cell membrane translocation of the N-terminal (1-28) part of the prion protein

P. Lundberg, M. Magzoub, M. Lindberg, M. Hällbrink, J. Jarvet, L. E.G. Eriksson, Ü Langel, A. Gräslund

Research output: Contribution to journalArticlepeer-review

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 (PrPSc) form of the protein and its amyloidic transformation.

Original languageEnglish (US)
Pages (from-to)85-90
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume299
Issue number1
DOIs
StatePublished - 2002

Keywords

  • Aggregation
  • Cell penetrating peptide
  • Membrane interaction
  • Prion protein N-terminus
  • β-Structure

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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