A simple in vitro assay for assessing the efficacy, mechanisms and kinetics of anti-prion fibril compounds.

ABSTRACT: Prion diseases are caused by the conversion of normal cellular prion proteins (PrP) into lethal prion aggregates. These prion aggregates are composed of proteinase K (PK) resistant fibrils and comparatively PK-sensitive oligomers. Currently there are no anti-prion pharmaceuticals available to treat or prevent prion disease. Methods of discovering anti-prion molecules rely primarily on relatively complex cell-based, tissue slice or animal-model assays that measure the effects of small molecules on the formation of PK-resistant prion fibrils. These assays are difficult to perform and do not detect the compounds that directly inhibit oligomer formation or alter prion conversion kinetics. We have developed a simple cell-free method to characterize the impact of anti-prion fibril compounds on b

SUBMITTER: Ladner-Keay CL 

PROVIDER: S-EPMC6277192 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature