A 1H NMR method for the analysis of antigen-antibody interactions: binding of a peptide fragment of lysozyme to anti-lysozyme monoclonal antibody.
A proton nuclear magnetic resonance (NMR) study is reported of the molecular structural basis of antigen-antibody interactions. An immunologically reactive proteolytic fragment corresponding to one of the antigenic regions on hen egg-white lysozyme (HEL) was used in combination with a monoclonal antibody that recognizes this site. Using spin diffusion, we prepared an antibody in which the magnetization of the antigen binding site was saturated by non-specific nuclear Overhauser effect. Under these conditions the effect of the saturation of the antibody was observed to spread over the peptide fragment through the antigen binding site. On the basis of the results obtained for the intermolecular nuclear Overhauser effect, we discuss how the peptide fragment interacts with the antibody. The side chains of aromatic residues, Trp, Tyr, and His, and of ionic residues, especially Arg, Lys, and Glu, are suggested to be important in the antigen-antibody interaction.
Department of Biophysics and Biochemistry, Faculty of Science, University of Tokyo.
W
W
Ito
M
M
Nishimura
N
N
Sakato
H
H
Fujio
Y
Y
Arata
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000937:Antigen-Antibody Reactions; D001666:Binding Sites, Antibody; D002645:Chickens; D003460:Crystallization; D004529:Egg White / Q000032:analysis; D009682:Magnetic Resonance Spectroscopy; D009113:Muramidase / Q000276:immunology*; D010446:Peptide Fragments / Q000276:immunology; D014961:X-Ray Diffraction
D000911:Antibodies, Monoclonal; D010446:Peptide Fragments; D009113:Muramidase