Single Molecule Force Spectroscopy to Compare Natural versus Artificial Antibody–Antigen Interaction

Congzhou Wang, Rong Hu, Jeremiah J. Morrissey, Evan D. Kharasch, Srikanth Singamaneni

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Biorecognition is central to various biological processes and finds numerous applications in virtually all areas of chemistry, biology, and medicine. Artificial antibodies, produced by imprinting synthetic polymers, are designed to mimic the biological recognition capability of natural antibodies, while exhibiting superior thermal, chemical, and environmental stability compared to their natural counterparts. The binding affinity of the artificial antibodies to their antigens characterizes the biorecognition ability of these synthetic nanoconstructs and their ability to replace natural recognition elements. However, a quantitative study of the binding affinity of an artificial antibody to an antigen, especially at the molecular level, is still lacking. In this study, using atomic force microscopy-based force spectroscopy, the authors show that the binding affinity of an artificial antibody to an antigen (hemoglobin) is weaker than that of natural antibody. The fine difference in the molecular interactions manifests into a significant difference in the bioanalytical parameters of biosensors based on these recognition elements.

Original languageEnglish
Article number1604255
JournalSmall
Volume13
Issue number19
DOIs
StatePublished - May 17 2017

Keywords

  • artificial antibodies
  • gold nanorods
  • molecular imprinting
  • plasmonic biosensor
  • surface force spectroscopy

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