H4:1 and H4:2 monoclonal antibodies discriminate between the normal and misfolded conformers of recombinant prion protein
type: CreativeWork
description: Prion diseases are infectious diseases and the causative agent of this disease is a misfolded conformer of prion protein which lack nucleic acids. For the last two decades prion diseases are still standing tall in front of science, neither a cure nor a proper diagnosis method are available until today. Most of the diagnosis methods which are available in the market are a combination of protease treatment and immunoassay. It would be highly advantageous if we can eliminate the proteinase treatment step. There are very few mAbs available in the market which do not require the PK step. In this project we tested two mAbs H4:1 and H4:2 which are selective against synthetic peptide made by the SDS method. Even the peptide made by this method is unglycosilated these mAbs clearly discriminated in between aggregated and monomeric peptides.
abstract: Prion diseases are infectious diseases and the causative agent of this disease is a misfolded conformer of prion protein which lack nucleic acids. For the last two decades prion diseases are still standing tall in front of science, neither a cure nor a proper diagnosis method are available until today. Most of the diagnosis methods which are available in the market are a combination of protease treatment and immunoassay. It would be highly advantageous if we can eliminate the proteinase treatment step. There are very few mAbs available in the market which do not require the PK step. In this project we tested two mAbs H4:1 and H4:2 which are selective against synthetic peptide made by the SDS method. Even the peptide made by this method is unglycosilated these mAbs clearly discriminated in between aggregated and monomeric peptides.
author: Panigrahy, Chinmaya Narayan
date published: 2010
date modified: 2026-07-24T04:50:29Z
provider: University of Strathclyde
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Strathclyde

PropertyValue
property ID: DOI
value: 10.48730/xkfb-nj89