Prion paper response - notrack changes.pdf (959.07 kB)
Rapid quantification of prion proteins using resistive pulse sensing
journal contribution
posted on 2020-02-13, 11:40 authored by Matthew Healey, Muttuswamy Sivakumaran, Mark PlattMark PlattPrion 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
AnalystVolume
145Issue
7Pages
2595-2601Publisher
Royal Society of ChemistryVersion
- AM (Accepted Manuscript)
Rights holder
© Royal Society of ChemistryPublisher 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
2020-02-11Publication date
2020-02-12Copyright date
2020ISSN
0003-2654eISSN
1364-5528Publisher version
Language
- en
Depositor
Dr Mark Platt. Deposit date: 12 February 2020Usage metrics
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