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Rapid quantification of prion proteins using resistive pulse sensing
journal contributionposted on 13.02.2020, 11:40 by Matthew Healey, Muttuswamy Sivakumaran, Mark Platt
Prion diseases are a group of fatal transmissible neurological conditions caused by the change in conformation of intrinsic cellular prion protein (PrPC). We present a rapid assay using Aptamers and Resistive Pulse Sensing, RPS, to extract and quantify PrPc 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 PrPc 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 PrPc protein. The process is done in under an hour and allows the detection of picomol’s of protein.
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