Folding analytical devices for electrochemical ELISA in hydrophobic R(H) paper. Academic Article uri icon

Overview

MeSH

  • Animals
  • Antibodies, Protozoan
  • Colorimetry
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Immunoglobulin G
  • Limit of Detection
  • Malaria, Falciparum
  • Plasmodium falciparum
  • Proteins
  • Rabbits

MeSH Major

  • Electrochemistry
  • Enzyme-Linked Immunosorbent Assay
  • Immobilized Proteins
  • Paper

abstract

  • This work describes a device for electrochemical enzyme-linked immunosorbent assay (ELISA) designed for low-resource settings and diagnostics at the point of care. The device is fabricated entirely in hydrophobic paper, produced by silanization of paper with decyl trichlorosilane, and comprises two zones separated by a central crease: an embossed microwell, on the surface of which the antigen or antibody immobilization and recognition events occur, and a detection zone where the electrodes are printed. The two zones are brought in contact by folding the device along this central crease; the analytical signal is recorded from the folded configuration. Two proof-of-concept applications, an electrochemical direct ELISA for the detection of rabbit IgG as a model antigen in buffer and an electrochemical sandwich ELISA for the detection of malarial histidine-rich protein from Plasmodium falciparum (Pf HRP2) in spiked human serum, show the versatility of this device. The limit of detection of the electrochemical sandwich ELISA for the quantification of Pf HRP2 in spiked human serum was 4 ng mL(-1) (10(2) pmol L(-1)), a value within the range of clinically relevant concentrations.

publication date

  • December 16, 2014

has subject area

  • Animals
  • Antibodies, Protozoan
  • Colorimetry
  • Electrochemistry
  • Enzyme-Linked Immunosorbent Assay
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Immobilized Proteins
  • Immunoglobulin G
  • Limit of Detection
  • Malaria, Falciparum
  • Paper
  • Plasmodium falciparum
  • Proteins
  • Rabbits

Research

keywords

  • Journal Article

Identity

Language

  • eng

Digital Object Identifier (DOI)

  • 10.1021/ac5020782

PubMed ID

  • 25470031

Additional Document Info

start page

  • 11999

end page

  • 12007

volume

  • 86

number

  • 24