Electron spin resonance studies on the lipid-protein interaction between cardiolipin and anti-cardiolipin antibodies.
Electron spin resonance measurements were performed in order to investigate the influence of anti-cardiolipin antibodies on cardiolipin-containing liposomes. The physical state of the lipid structures and the alterations caused by the interaction with specific antibody were determined by measuring the freedom of motion of spin-labeled stearic acid derivatives incorporated into the lipid structures. The interaction of the cardiolipin-containing liposomes with the anti-cardiolipin antibodies reduced the mobility of the spin-labeled stearic acid probe I (12, 3), whose nitroxide group is assumed to be located near the polar region of the lipid bilayer. The restricted mobility, which qualitatively resembles the interaction of cardiolipin liposomes with calcium ions, is probably the result of a tighter packing of the polar groups in their crystalline array. The binding sites of the cardiolipin structures for anti-cardiolipin antibodies and Ca2 ions seem to be identical. As indicated by the spin-labeled stearic acid probe I (1, 14), the apolar region of the lipid bilayer is not affected by the interaction of the cardiolipin-containing liposomes with the anti-cardiolipin antibodies.
D000937:Antigen-Antibody Reactions; D001665:Binding Sites; D002308:Cardiolipins / Q000276:immunology*; D004578:Electron Spin Resonance Spectroscopy; D007114:Immunization; D007136:Immunoglobulins; D008081:Liposomes; D008968:Molecular Conformation; D011485:Protein Binding; D011487:Protein Conformation; D013229:Stearic Acids; D013997:Time Factors
D002308:Cardiolipins; D007136:Immunoglobulins; D008081:Liposomes; D013229:Stearic Acids