Colorimetric aptasensor for Campylobacter jejuni cells by exploiting the peroxidase like activity of Au@Pd nanoparticles

Mikrochim Acta. 2018 Sep 5;185(10):448. doi: 10.1007/s00604-018-2976-2.

Abstract

The authors describe a method for colorimetric determination of Campylobacter jejuni (C. jejuni) in milk samples. It is based on the interaction of a specific DNA aptamer with surface protein in the cell membranes of C. jejuni. Specific binding of the aptamer with the cell membrane leads to an uptake of aptamer from solution. As a result, the concentration of aptamer floating in the solution is reduced. In the presence of large quantities of aptamer, the surface of added Au@Pd nanoparticles (NPs) is covered with aptamer via electrostatic interactions. Hence, they cannot act as a peroxidase mimic and oxidize the substrate 3,3',5,5'-tetramethylbenzidine (TMB) to give a blue product. However, when the aptamer is bound by the target cells, the surface of the NPs is not blocked by aptamer and the NPs exert a strong peroxidase -like activity. Under defined experimental conditions, the intensity of the blue color increases with the concentration of C. jejuni, and as little as 100 CFU·mL-1 can bedetected in milk. Graphical abstract A colorimetric aptasensor for assay Campylobacter jejuni whole cell in food samples was investigated. This assay was designed based on interaction of specific DNA aptamer with surface protein in c. jejuni cell membrane without any modification of aptamer.

Keywords: Bacteria; Colorimetry; DNA aptamer; Enzyme mimic; Milk.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aptamers, Nucleotide / chemistry
  • Aptamers, Nucleotide / metabolism*
  • Base Sequence
  • Biomimetic Materials / chemistry
  • Biosensing Techniques / methods*
  • Campylobacter jejuni / isolation & purification*
  • Colorimetry
  • Gold / chemistry*
  • Metal Nanoparticles / chemistry*
  • Palladium / chemistry*
  • Peroxidases / metabolism*

Substances

  • Aptamers, Nucleotide
  • Palladium
  • Gold
  • Peroxidases