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Rapid Quantification of Prion Proteins

submitted on 29.11.2019, 18:17 and posted on 09.12.2019, 09:20 by Matthew Healey, Muttuswamy Sivakumaran, Mark Platt

Prion diseases are a group of fatal transmissible neurological conditions caused by the change in conformation of the normal intrinsic cellular prion protein (PrPC) in to the highly ordered insoluble amyloid state conformer (PrPSC). We present a rapid assay using Aptamers and Resistive Pulse Sensing, RPS, to extract and quantify proteins from complex sample matrices, demonstrate with the quantification of PrPc. 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. The technique could be easily adopted to the mutated version of the protein and integrated into clinical workflows for the screening of blood donations and transfusions.


Email Address of Submitting Author


Loughborough University


United Kingdom

ORCID For Submitting Author


Declaration of Conflict of Interest


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