Rapid presymptomatic detection of PrPSc via conformationally responsive palindromic PrP peptides.
Structurally unique, synthetic prion peptides provide the basis of a simple assay to serve as both a detection and signal amplification system that distinguishes the normal prion protein, PrPC, from the misfolded prion protein, PrPSc, that is associated with the occurrence of transmissible spongiform encephalopathies (TSE). Proof-of-principle has been shown on brain samples from an experimental scrapie hamster model. The assay demonstrates very sensitive detection of PrPSc in animal brain tissue with potential application for early presymptomatic detection in animal screening. Furthermore, the sensitivity of the assay could enable blood tests for this TSE disease as well as other amyloid and/or misfolded protein diseases.
Grosset
A
A
Department of Biochemistry and Molecular Biology, Georgetown University, Washington, DC 20006, USA.
Moskowitz
K
K
Nelsen
C
C
Pan
T
T
Davidson
E
E
Orser
C S
CS
D000818:Animals; D001681:Biological Assay; D001923:Brain Chemistry; D006224:Cricetinae; D005260:Female; D006801:Humans; D008647:Mesocricetus; D010455:Peptides / Q000032:analysis*; D018620:PrPSc Proteins / Q000032:analysis*; D017096:Prion Diseases / Q000175:diagnosis; D017510:Protein Folding; D012680:Sensitivity and Specificity
D010455:Peptides; D018620:PrPSc Proteins