Specific antigen/antibody interactions measured by force microscopy.
Molecular recognition between biotinylated bovine serum albumin and polyclonal, biotin-directed IG antibodies has been measured directly under various buffer conditions using an atomic force microscope (AFM). It was found that even highly structured molecules such as IgG antibodies preserve their specific affinity to their antigens when probed with an AFM in the force mode. We could measure the rupture force between individual antibody-antigen complexes. The potential and limitations of this new approach for the measurement of individual antigen/antibody interactions and some possible applications are discussed.
Dammer
U
U
Institute of Physics, University of Basel, Basel, Switzerland.
Hegner
M
M
Anselmetti
D
D
Wagner
P
P
Dreier
M
M
Huber
W
W
Güntherodt
H J
HJ
D000936:Antigen-Antibody Complex / Q000648:ultrastructure*; D000937:Antigen-Antibody Reactions; D001666:Binding Sites, Antibody; D002021:Buffers; D007074:Immunoglobulin G / Q000276:immunology* / Q000648:ultrastructure*; D018625:Microscopy, Atomic Force / Q000379:methods; D008961:Models, Structural; D012710:Serum Albumin, Bovine / Q000276:immunology* / Q000648:ultrastructure*
D000936:Antigen-Antibody Complex; D002021:Buffers; D007074:Immunoglobulin G; D012710:Serum Albumin, Bovine