UV-Light Exposed Prion Protein Fails to Form Amyloid Fibrils
Author Information
Author(s): Abhay Kumar Thakur, Ch Mohan Rao
Primary Institution: Centre for Cellular and Molecular Biology, Council of Scientific and Industrial Research, Hyderabad, India
Hypothesis
Does UV exposure affect the ability of prion protein to form amyloid fibrils?
Conclusion
UV-exposed prion protein fails to form amyloid fibrils but can extend fibrils when provided with pre-formed fibril seeds.
Supporting Evidence
- UV-exposed prion protein shows a significant decrease in helicity.
- ThT fluorescence indicates that UV-exposed prion protein does not form amyloid fibrils de novo.
- UV-exposed prion protein can extend fibrils when provided with pre-formed fibril seeds.
Takeaway
When prion protein is exposed to UV light, it can't make new amyloid fibrils by itself, but it can still grow on existing ones if they are provided.
Methodology
The study involved exposing mouse full-length prion protein to UV light and analyzing its ability to form amyloid fibrils under various conditions.
Limitations
The study does not explore the long-term effects of UV exposure on prion protein or its implications in vivo.
Statistical Information
P-Value
p<0.005
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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