Related Experiment Video
Updated: Apr 15, 2026

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain
Published on: October 3, 2012
The Unexposed Secrets of Prion Protein Oligomers
Gailing Wang1, Mingcheng Wang2, Chuanfeng Li2
1Department of Bioengineering, Huanghuai University, 463000, Zhumadian, China. wgl939@126.com.
Abstract:
According to the "protein-only" hypothesis, the misfolding and conversion of host-derived cellular prion protein (PrP(C)) into pathogenically misfolded PrP are believed to be the key procedure in the pathogenesis of prion diseases. Intermediate, soluble oligomeric prion protein (PrP) aggregates were considered a critical process for prion diseases. Several independent studies on PrP oligomers gained insights into oligomers' formation, biophysical and biochemical characteristics, structure conversion, and neurotoxicity. PrP oligomers are rich in β-sheet structure and slightly resistant to proteinase K digestion. PrP oligomers exhibited more neurotoxicity and induced neuronal apoptosis in vivo and/or in vitro. In this review, we summarized recent studies regarding PrP oligomers and the relationship between misfolded PrP aggregates and neuronal death in the course of prion diseases.
More Related Videos
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid Fibrils
Molecular Chaperones and Protein Folding
The...
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein Folding

