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Single Molecule Force Spectroscopy to Compare Natural versus Artificial Antibody–Antigen Interaction
Author(s) -
Wang Congzhou,
Hu Rong,
Morrissey Jeremiah J.,
Kharasch Evan D.,
Singamaneni Srikanth
Publication year - 2017
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201604255
Subject(s) - force spectroscopy , molecular recognition , biosensor , antigen , antibody , chemistry , nanotechnology , bioanalysis , molecule , biophysics , atomic force microscopy , materials science , biology , immunology , organic chemistry
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.