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Rapid quantification of prion proteins using resistive pulse sensing

journal contribution
posted 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.

History

School

  • Science

Department

  • Chemistry

Published in

Analyst

Volume

145

Issue

7

Pages

2595-2601

Publisher

Royal Society of Chemistry

Version

AM (Accepted Manuscript)

Rights holder

© Royal Society of Chemistry

Publisher statement

This paper was accepted for publication in the journal Analyst and the definitive published version is available at https://doi.org/10.1039/D0AN00063A.

Acceptance date

11/02/2020

Publication date

2020-02-12

Copyright date

2020

ISSN

0003-2654

eISSN

1364-5528

Language

en

Depositor

Dr Mark Platt. Deposit date: 12 February 2020

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