Literature DB >> 16269350

Rapid presymptomatic detection of PrPSc via conformationally responsive palindromic PrP peptides.

A Grosset1, K Moskowitz, C Nelsen, T Pan, E Davidson, C S Orser.   

Abstract

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.

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Year:  2005        PMID: 16269350     DOI: 10.1016/j.peptides.2005.03.006

Source DB:  PubMed          Journal:  Peptides        ISSN: 0196-9781            Impact factor:   3.750


  4 in total

1.  Computer simulation study of amyloid fibril formation by palindromic sequences in prion peptides.

Authors:  Victoria A Wagoner; Mookyung Cheon; Iksoo Chang; Carol K Hall
Journal:  Proteins       Date:  2011-05-09

2.  Structure-selective anisotropy assay for amyloid Beta oligomers.

Authors:  Evgenia G Matveeva; Alan Rudolph; Jonathan R Moll; Richard B Thompson
Journal:  ACS Chem Neurosci       Date:  2012-08-18       Impact factor: 4.418

Review 3.  Identification of misfolded proteins in body fluids for the diagnosis of prion diseases.

Authors:  Francesca Properzi; Maurizio Pocchiari
Journal:  Int J Cell Biol       Date:  2013-08-21

4.  Detection and control of prion diseases in food animals.

Authors:  Peter Hedlin; Ryan Taschuk; Andrew Potter; Philip Griebel; Scott Napper
Journal:  ISRN Vet Sci       Date:  2012-02-29
  4 in total

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