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Single antibody-antigen interactions monitored via transient ionic current recording using nanopore sensors.

Yi-Lun YingYi-Tao LongYong-Xu HuRui GaoYi-Tao Long
Published in: Chemical communications (Cambridge, England) (2018)
Understanding the single molecular protein-protein interaction has great significance in evaluating the affinity of a specific antibody. Herein, the interaction between single α-fetal protein (AFP) and its antibody was monitored via transient ionic current recording by using the antibody functionalized nanopore sensors. More importantly, the kinetic evaluation was performed at the single molecule level to determine the dissociation constant of this interaction. This method enables the monitoring of the kinetic antigen-antibody interaction in their heterogenetic state without any labelling. Our results provided new insights into the evaluation of the antibody's binding affinity and more into the development of immunoassays for diagnostics.
Keyphrases
  • single molecule
  • protein protein
  • small molecule
  • atomic force microscopy
  • quantum dots
  • solid state
  • high resolution
  • binding protein
  • molecularly imprinted
  • solid phase extraction