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Real-time Quaking-induced Conversion Assay for Detection of CWD Prions in Fecal Material

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Published on: September 29, 2017

Rapid quantification of prion proteins using resistive pulse sensing.

Matthew J Healey¹, Muttuswamy Sivakumaran, Mark Platt

¹Department of Chemistry, Loughborough University, Loughborough, Leicestershire, LE11 3TU, UK. m.platt@lboro.ac.uk.

|February 18, 2020

Summary

This study introduces a fast aptamer-based assay using resistive pulse sensing (RPS) to detect prion diseases. The novel method efficiently quantifies the prion protein (PrP^C) in complex samples within an hour.

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Area of Science:

Neuroscience
Biotechnology
Analytical Chemistry

Background:

Prion diseases are fatal neurodegenerative disorders.
These conditions arise from misfolded cellular prion protein (PrP^C).
Accurate quantification of PrP^C is crucial for diagnosis and research.

Purpose of the Study:

To develop a rapid and sensitive assay for PrP^C detection.
To quantify PrP^C in complex biological matrices.
To enable early detection and monitoring of prion diseases.

Main Methods:

Functionalization of superparamagnetic beads (SPBs) with DNA aptamers.
Pre-concentration of PrP^C using aptamer-modified P-beads.
Quantification of eluted PrP^C via aptamer-modified S-beads and resistive pulse sensing (RPS).

Main Results:

The assay successfully extracts and quantifies PrP^C from complex samples.
The method achieves detection limits in the picomolar range.
The entire process is completed in under one hour.

Conclusions:

The aptamer-RPS assay offers a rapid and sensitive method for PrP^C quantification.
This technique has potential applications in diagnosing and studying prion diseases.
The assay's speed and sensitivity represent a significant advancement in prion protein detection.