Rapid quantification of prion proteins using resistive pulse sensing

Analyst. 2020 Apr 7;145(7):2595-2601. doi: 10.1039/d0an00063a. Epub 2020 Feb 17.

Abstract

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.

MeSH terms

  • Aptamers, Nucleotide / chemistry
  • Aptamers, Nucleotide / metabolism
  • Biosensing Techniques / methods*
  • Humans
  • Magnetics
  • Nanopores
  • Prion Proteins / analysis*
  • Prion Proteins / genetics
  • Prion Proteins / metabolism
  • Recombinant Proteins / analysis*
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Temperature

Substances

  • Aptamers, Nucleotide
  • Prion Proteins
  • Recombinant Proteins