Inhibition of phosphorylcholine binding to antibodies using synthetic peptides.
The amino-acid sequence Phe-Tyr-Met-Glu is unique to phosphorylcholine (PC)-binding antibodies. It occurs in the first complementarity-determining region (CDR1) of the immunoglobulin heavy chains in 89% of all the anti-PC myeloma and hybridoma proteins but is not present in 490 other immunoglobulin heavy chains, 854 light chains or in 2,260 other unrelated proteins. This unique tetrapeptide therefore seems to be involved in PC binding. Here we compare the effectiveness of Phe-Tyr-Met-Glu and other structurally related peptides in inhibiting the binding of PC to PC-binding proteins McPC603 and HOPC8. We also test a surface-simulation peptide that was constructed to mimic the combining site of McPC603. Our data suggest that all these peptides inhibit the binding of PC to PC-binding proteins non-specifically and we show by computer modelling that the surface-simulation peptide does not duplicate the combining site of McPC603.
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000276:immunology; D001666:Binding Sites, Antibody; D001667:Binding, Competitive; D002794:Choline / Q000031:analogs & derivatives*; D008958:Models, Molecular; D009842:Oligopeptides / Q000276:immunology*; D010767:Phosphorylcholine / Q000276:immunology*; D011487:Protein Conformation
D000911:Antibodies, Monoclonal; D009842:Oligopeptides; D010767:Phosphorylcholine; D002794:Choline