Force-Induced Selective
Dissociation of Noncovalent
Antibody–Antigen Bonds
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Abstract
Specific noncovalent binding between antibody and antigen
molecules
is the basis for molecular recognition in biochemical processes. Quantitative
investigation of the binding forces could lead to molecular specific
analysis and potentially mechanical manipulation of these processes.
Using our force-induced remnant magnetization spectroscopy, we revealed
a well-defined binding force for the bonds between mouse immunoglobulin
G and magnetically labeled α-mouse immunoglobulin G. The force
was calibrated to be 120 ± 15 pN. In comparison, the binding
force was only 17 ± 3 pN for physisorption and much higher than
120 pN for biotin–streptavidin bonds. A unique rebinding method
was used to confirm the dissociation of the antibody–antigen
bonds. A well-defined and molecule-specific binding force opens a
new avenue for distinguishing different noncovalent bonds in biochemical
processes