Rapid quantification of prion proteins using resistive pulse sensing

Abstract

Prion diseases are a group of fatal transmissible neurological conditions caused by the change in conformation of intrinsic cellular prion protein (PrP^C). We present a rapid assay using aptamers and resistive pulse sensing, RPS, to extract and quantify PrP^C from complex sample matrices. We functionalise the surface of superparamagnetic beads, SPBs, with a DNA aptamer. First SPB's termed P-beads, are used to pre-concentrate the analyte from a large sample volume. The PrP^C protein is then eluted from the P-beads before aptamer modified sensing beads, S-beads, are added. The velocity of the S-beads through the nanopore reveals the concentration of the PrP^C protein. The process is done in under an hour and allows the detection of picomol's of protein.