ArticleThe journal of physical chemistry. B2012
Dissecting structure of prion amyloid fibrils by hydrogen-deuterium exchange ultraviolet Raman spectroscopy.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- Development of a rapid and novel diagnostic technique for cardiac amyloidosis using Raman spectroscopy.Research square · 2025Article
- A Review on Integrated ZnO-Based SERS Biosensors and Their Potential in Detecting Biomarkers of Neurodegenerative Diseases.Biosensors · 2023Review
- From Research to Diagnostic Application of Raman Spectroscopy in Neurosciences: Past and Perspectives.Free neuropathology · 2022Article
- Ultraviolet Resonance Raman Spectroscopic Markers for Protein Structure and Dynamics.Trends in analytical chemistry : TRAC · 2018Article
- Amyloid fibrils: the eighth wonder of the world in protein folding and aggregation.Biophysical journal · 2014Article
- Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification.The Journal of biological chemistry · 2013Article
- Defining the conformational features of anchorless, poorly neuroinvasive prions.PLoS pathogens · 2013Article
- Switching in amyloid structure within individual fibrils: implication for strain adaptation, species barrier and strain classification.FEBS letters · 2009Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The molecular mechanisms underlying structural diversity of amyloid fibrils or prion strains formed within the same primary structure is considered to be one of the most enigmatic questions in prion biology. We report here on the direct characterization of amyloid structures using a novel spectroscopic technique, hydrogen-deuterium exchange ultraviolet Raman spectroscopy. This method enables us to assess the structural differences within highly ordered cross-β-cores of two amyloid states produced within the same amino acid sequence of full-length mammalian prion protein. We found that while both amyloid states consisted of β-structures, their cross-β-cores exhibited hydrogen bonding of different strengths. Moreover, Raman spectroscopy revealed that both amyloid states displayed equally narrow crystalline-like bands, suggesting uniform structures of cross-β-cores within each state. Taken together, these data suggest that highly polymorphous fibrils can display highly uniform structures of their cross-β-core and belong to the same prion strain.
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Registered trials
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