Characterizing affinity epitopes between prion protein and β-amyloid using an epitope mapping immunoassay.

ABSTRACT: Cellular prion protein, a membrane protein, is expressed in all mammals. Prion protein is also found in human blood as an anchorless protein, and this protein form is one of the many potential sources of misfolded prion protein replication during transmission. Many studies have suggested that β-amyloid1-42 oligomer causes neurotoxicity associated with Alzheimer's disease, which is mediated by the prion protein that acts as a receptor and regulates the hippocampal potentiation. The prevention of the binding of these proteins has been proposed as a possible preventative treatment for Alzheimer's disease; therefore, a greater understanding of the binding hot-spots between the two molecules is necessary. In this study, the epitope mapping immunoassay was employed to characterize binding epitop

SUBMITTER: Kang M 

PROVIDER: S-EPMC3789258 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature