@article{3013233,
    title = "The position of the LysN(ε)H2-grafted antigens along the sequential oligopeptide carrier, Ac-(Aib-Lys-Aib-Gly)(n) (SOC(n)-II), influences the antibody recognition: Application to the Sm main autoimmune epitope",
    author = "Alexopoulos, C. and Tsikaris, V. and Rizou, C. and Sakarellos-Daitsiotis, M. and Sakarellos, C. and Cung, M.T. and Marraud, M. and Vlachoyiannopoulos, P.G. and Moutsopoulos, H.M.",
    journal = "Biopolymers - Biospectroscopy Section",
    year = "2000",
    volume = "54",
    number = "1",
    pages = "1-10",
    publisher = "John Wiley & Sons Inc, New York, NY, United States",
    doi = "10.1002/(SICI)1097-0282(200007)54:1<1::AID-BIP10>3.0.CO;2-7",
    keywords = "Conformations;  Fourier transform infrared spectroscopy;  Nuclear magnetic resonance spectroscopy;  Samarium;  Substrates, Antigenic peptides;  Sequential oligopeptide carrier, Antigens, autoantibody;  autoantigen;  carrier protein;  epitope;  lysine;  oligopeptide;  polymer;  ribonucleoprotein;  antigen;  peptide fragment;  Sm nuclear antigens;  small nuclear ribonucleoprotein, antibody detection;  antibody specificity;  article;  autoimmune disease;  conformation;  mixed connective tissue disease;  polymerization;  protein structure;  sequence analysis;  systemic lupus erythematosus;  amino acid sequence;  animal;  cattle;  chemistry;  human;  immunology;  molecular genetics;  synthesis, Amino Acid Sequence;  Animals;  Antigens;  Autoantibodies;  Autoantigens;  Carrier Proteins;  Cattle;  Epitopes;  Humans;  Lysine;  Molecular Sequence Data;  Oligopeptides;  Peptide Fragments;  Ribonucleoproteins, Small Nuclear",
    abstract = "A sequential oligopeptide carrier of antigenic peptides is presented, incorporating two Aib residues in each repetitive moiety: Ac-(Aib-Lys-Aib- Gly)(n) (SOC(n)-II; n = 2-4). The conformational study, by 1H-nmr, CD, and Fourier transform ir spectroscopy, indicated that the SOC(n)-II carrier displays a pronounced 310-helix, compared to the Ac-(Lys-Aib-Gly)(n) (SOC(n)-I) carrier of the same approximately backbone length, previously reported. One of the dominant autoimmune epitopes of the Sm and U1RNP cellular components, the PPGMRPP sequence, was coupled to the Lys-N(ε)H2 groups of the SOC(n)-II carrier and used as antigenic substrate for detecting anti-Sm/U1RNP autoantibodies in ELISA assays. Anti-Sm antibodies are highly specific for systemic lupus erythematosus, while anti-U1RNP are specific for mixed connective tissue disease. The anti-(PPGMRPP)5-SOC(n)-II ELISA was compared with the anti-(PPGMRPP)(n)-SOC(n)-I ELISA, provided that both antigenic substrates possess the same amount of the epitope replicates. The significance of the lysine positions along the oligopeptide backbone of the carrier for a favorable antibody recognition of the anchored antigens is also examined. (C) 2000 John Wiley and Sons, Inc.
A sequential oligopeptide carrier of antigenic peptides is presented, incorporating two Aib residues in each repetitive moiety: Ac-(Aib-Lys-Aib-Gly)n (SOCn-II; n = 2-4). The conformational study, by 1H-nmr, CD, and Fourier transform ir spectroscopy, indicated that the SOCn-II carrier displays a pronounced 310-helix, compared to the Ac-(Lys-Aib-Gly)n (SOCn-I) carrier of the same approximately backbone length, previously reported. One of the dominant autoimmune epitopes of the Sm and U1RNP cellular components, the PPGMRPP sequence, was coupled to the Lys-NεH2 groups of the SOCn-II carrier and used as antigenic substrate for detecting anti-Sm/U1RNP autoantibodies in ELISA assays. Anti-Sm antibodies are highly specific for systemic lupus erythematosus, while anti-U1RNP are specific for mixed connective tissue disease. The anti-(PPGMRPP)5-SOCn-II ELISA was compared with the anti-(PPGMRPP)n-SOCn-I ELISA, provided that both antigenic substrates possess the same amount of the epitope replicates. The significance of the lysine positions along the oligopeptide backbone of the carrier for a favorable antibody recognition of the anchored antigens is also examined."
}