Force-induced selective dissociation of noncovalent antibody-antigen bonds
1Department of Chemistry, University of Houston, Houston, Texas 77204, USA.
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.
Related Concept Videos
Drug-Receptor Bonds
In...
Antibody Actions
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
Ligand Binding Sites
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Affinity and Avidity
Noncovalent Attractions in Biomolecules
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Affinity Chromatography


