Specific antigen/antibody interactions measured by force microscopy.
AUTOR(ES)
Dammer, U
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=1225221Documentos Relacionados
- Detection and localization of individual antibody-antigen recognition events by atomic force microscopy.
- DNA bending by photolyase in specific and non-specific complexes studied by atomic force microscopy.
- The relationship between ligand-binding thermodynamics and protein-ligand interaction forces measured by atomic force microscopy.
- Quantitation of antibody to hepatitis A antigen by immune electron microscopy.
- The role of circulating hepatitis B antigen/antibody immune complexes in the pathogenesis of vascular and hepatic manifestations in polyarteritis nodosa