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- W2005241531 abstract "The multiphosphorylated tryptic peptide αs1-casein(59–79) has been shown to be antigenic with anti-casein antibodies. In an approach to determine the amino acyl residues critical for antibody binding we undertook an epitope analysis of the peptide using overlapping synthetic peptides. With αs1-casein(59–79) as the adsorbed antigen in a competitive ELISA only two of five overlapping synthetic peptides at 1 mM significantly inhibited binding of the anti-casein antibodies. Peptides Glu-Ser(P)-Ile-Ser(P)-Ser(P)-Ser(P)-Glu-Glu and Ile-Val-Pro-Asn-Ser(P)-Val-Glu-Glu inhibited antibody binding by 20.0±3.6% and 60.3±7.9%, respectively. The epitope of Glu63-Ser(P)-Ile-Ser(P)-Ser(P)-Ser(P)-Glu-Glu70 was further localised to the phosphoseryl cluster as the peptide Ser(P)-Ser(P)-Ser(P) significantly inhibited binding of the anti-casein antibodies to αs1-casein(59–79) by 29.5±7.4%. Substitution of Ser(P)75 with Ser75 in the second inhibitory peptide Ile-Val-Pro-Asn-Ser(P)75-Val-Glu-Glu also abolished inhibition of antibody binding to αs1-casein (59–79) demonstrating that Ser(P)75 is also a critical residue for recognition by the antibodies. These data show that the phosphorylated residues in the cluster sequence -Ser(P)66-Ser(P)-Ser(P)68 and in the sequence -Pro73-Asn-Ser(P)-Val-Glu77- are critical for antibody binding to αs1-casein(59–79) and further demonstrate that a highly phosphorylated segment of a protein can be antigenic. Copyright © 1999 European Peptide Society and John Wiley & Sons, Ltd." @default.
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- W2005241531 date "1999-05-01" @default.
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- W2005241531 title "Epitope analysis of the multiphosphorylated peptide αs1-casein(59-79)" @default.
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- W2005241531 doi "https://doi.org/10.1002/(sici)1099-1387(199905)5:5<221::aid-psc182>3.0.co;2-o" @default.
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