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The pH-triggered conversion of the PrP(c) to PrP(sc.).
1Gordon Life Science Institute, 53 South Cottage Road, Belmont, MA 02478, USA. gpzhou@gordonlifescience.org
Current Topics in Medicinal Chemistry
|May 8, 2013
Summary
Transmissible spongiform encephalopathies are prion protein misfolding diseases. This review explores prion protein conversion mechanisms, focusing on structural intermediates and stability, aiding understanding of these neurodegenerative conditions.
Area of Science:
- Neuroscience
- Biochemistry
- Structural Biology
Background:
- Transmissible spongiform encephalopathies (TSEs) result from prion protein (PrP) misfolding and aggregation.
- The normal cellular prion protein (PrP(c)) converts to the abnormal, aggregated form (PrP(sc)) in the central nervous system.
- Characterizing PrP(c) is challenging due to its size and insolubility.
Purpose of the Study:
- To review current knowledge on PrP(c) to PrP(sc) conversion mechanisms.
- To elucidate the role of structural intermediates in prion diseases.
- To provide insights into the stability and structural dynamics of prion protein forms.
Main Methods:
- Review of existing literature on prion protein misfolding.
- Analysis of factors influencing PrP(c) to PrP(sc) conversion, including pH and denaturing conditions.
- Discussion of Nuclear Magnetic Resonance (NMR) data for structural characterization.
Main Results:
- Identified key questions regarding PrP(c) stability, low pH-induced conversion, and intermediate structures.
- Highlighted the detection and assay of premolten and β-oligomer intermediates.
- Introduced Chou's wenxiang diagram for visualizing prion protein structures.
Conclusions:
- Understanding prion protein conversion mechanisms is crucial for comprehending TSEs.
- Structural intermediates play a significant role in the misfolding pathway.
- Further research into PrP folding and aggregation is warranted.
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