Two large immunogenic and antigenic myoglobin peptides and the effects of cyclisation.
Peptides corresponding to sequences (72-88) and (26-54) of beef myoglobin have been synthesised in their open-chain and cyclised forms (using a disulphide bridge) and tested for their antigenicity and immunogenicity. Antibodies raised to beef myoglobin bound to both peptides but more strongly to the 29-residue than to the 17-residue peptide. Cyclisation increased the antigenicity of the larger peptide. In this form the peptide competed much more strongly than in the uncyclised form for specific antibodies to beef myoglobin. The peptides are immunogenic in mice without being coupled to a protein carrier and produce antibodies which bind to beef myoglobin. Peptide (26-54) is the more immunogenic in producing a larger antibody titre to the parent myoglobin and cyclisation again enhances this property. The findings lend weight to the view that longer peptide sequences might be expected to favour the folded state, therefore binding more strongly to antibodies raised to the native protein and eliciting a population of antibodies which contain a larger proportion specific for that conformation. Cyclisation enhances antigenicity and immunogenicity presumably by decreasing the number of degrees of conformational freedom of a peptide without excluding native-like conformations.
D000595:Amino Acid Sequence; D000818:Animals; D000917:Antibody Formation; D000937:Antigen-Antibody Reactions; D001667:Binding, Competitive; D003500:Cyclization; D009211:Myoglobin / Q000276:immunology*; D010455:Peptides / Q000276:immunology*; D011817:Rabbits; D013057:Spectrum Analysis
D009211:Myoglobin; D010455:Peptides