A surface protein-imprinted biosensor based on boronate affinity for the detection of anti-human immunoglobulin G

Mikrochim Acta. 2022 Feb 15;189(3):106. doi: 10.1007/s00604-022-05204-w.

Abstract

A surface protein-imprinted biosensor was constructed on a screen-printed carbon electrode (SPCE) for the detection of anti-human immunoglobulin G (anti-IgG). The SPCE was successively decorated with aminated graphene (NH2-G) and gold nanobipyramids (AuNBs) for signal amplification. Then 4-mercaptophenylboric acid (4-MPBA) was covalently anchored to the surface of AuNBs for capturing anti-IgG template through boronate affinity binding. The decorated SPCE was then deposited with an imprinting layer generated by the electropolymerization of pyrrole. After removal of the anti-IgG template by the dissociation of the boronate ester in an acidic solution, three-dimensional (3D) cavities complementary to the anti-IgG template were formed in the imprinting layer of polypyrrole (PPy). The molecularly imprinted polymers (MIP)-based biosensor was used for the detection of anti-IgG, exhibiting a wide linear range from 0.05 to 100 ng mL-1 and a low limit of detection of 0.017 ng mL-1 (S/N = 3). In addition, the MIP-based anti-IgG biosensor also shows high selectivity, reproducibility and stability. Finally, the practicability of the fabricated anti-IgG biosensor was demonstrated by accurate determination of anti-IgG in serum sample.

Keywords: Anti-IgG; Boronate affinity; Gold nanobipyramids; Molecularly imprinted polymers; Surface imprinting.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biosensing Techniques*
  • Borates / chemistry*
  • Electrochemical Techniques
  • Ferricyanides / chemistry*
  • Humans
  • Immunoglobulin G / analysis*
  • Membrane Proteins / chemistry*
  • Molecular Imprinting*

Substances

  • Borates
  • Ferricyanides
  • Immunoglobulin G
  • Membrane Proteins