Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization.

Journal article

Prion diseases are associated with a major refolding event of the normal cellular prion protein, PrP(C), where the predominantly alpha-helical and random coil structure of PrP(C) is converted into a beta-sheet-rich aggregated form, PrP(Sc). Under normal physiological conditions PrP(C) is attached to the outer leaflet of the plasma membrane via a GPI anchor, and it is plausible that an interaction between PrP and lipid membranes could be involved in the conversion of PrP(C) into PrP(Sc). Recom...

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Authors: Kazlauskaite, J; Sanghera, N; Sylvester, I; Vénien-Bryan, C; Pinheiro, T

• Publication status: Published
• Journal: Biochemistry
• Volume: 42
• Issue: 11
• Pages: 3295-3304
• Publication date: 2003-03-01
• DOI: 10.1021/bi026872q
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Protein Conformation; Microscopy, Electron; Membrane Lipids; Spectroscopy, Fourier Transform Infrared; PrPC Proteins; Recombinant Proteins; Cricetinae; Animals; Mesocricetus; Protein Folding