An unusual soluble beta-turn-rich conformation of prion is involved in fibril formation and toxic to neuronal cells.

Journal article

A key molecular event in prion diseases is the conversion of the prion protein (PrP) from its normal cellular form (PrPC) to the disease-specific form (PrPSc). The transition from PrPC to PrPSc involves a major conformational change, resulting in amorphous protein aggregates and fibrillar amyloid deposits with increased beta-sheet structure. Using recombinant PrP refolded into a beta-sheet-rich form (beta-PrP) we have studied the fibrillization of beta-PrP both in solution and in association ...

Expand abstract

Authors: Kazlauskaite, J; Young, A; Gardner, C; Macpherson, J; Vénien-Bryan, C

• Publication status: Published
• Journal: Biochemical and biophysical research communications
• Volume: 328
• Issue: 1
• Pages: 292-305
• Publication date: 2005-03-01
• DOI: 10.1016/j.bbrc.2004.12.172
• EISSN: 1090-2104
• ISSN: 0006-291X
• Language: English
• Keywords: Dose-Response Relationship, Drug; Animals; Structure-Activity Relationship; Neurons; Protein Conformation; Multienzyme Complexes; Dimerization; Neurotoxins; Cell Line, Tumor; Protein Structure, Secondary; Prions; Neuroblastoma; Cell Survival; Cricetinae; Rats; Mesocricetus; Solubility