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

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Wang, C; Hu, R; Morrissey, JJ; Kharasch, ED; Singamaneni, S

Published Date

  • May 2017

Published In

Volume / Issue

  • 13 / 19

PubMed ID

  • 28322497

Pubmed Central ID

  • PMC5776662

Electronic International Standard Serial Number (EISSN)

  • 1613-6829

Digital Object Identifier (DOI)

  • 10.1002/smll.201604255


  • eng

Conference Location

  • Germany